BMC Structural Biology最新文献

{"title":"Free fatty acid receptors: structural models and elucidation of ligand binding interactions","authors":"Irina G. Tikhonova,&nbsp;Elena Poerio","doi":"10.1186/s12900-015-0044-2","DOIUrl":"https://doi.org/10.1186/s12900-015-0044-2","url":null,"abstract":"<p>The free fatty acid receptors (FFAs), including FFA1 (orphan name: GPR40), FFA2 (GPR43) and FFA3 (GPR41) are G protein-coupled receptors (GPCRs) involved in energy and metabolic homeostasis. Understanding the structural basis of ligand binding at FFAs is an essential step toward designing potent and selective small molecule modulators.</p><p>We analyse earlier homology models of FFAs in light of the newly published FFA1 crystal structure co-crystallized with TAK-875, an ago-allosteric ligand, focusing on the architecture of the extracellular binding cavity and agonist-receptor interactions. The previous low-resolution homology models of FFAs were helpful in highlighting the location of the ligand binding site and the key residues for ligand anchoring. However, homology models were not accurate in establishing the nature of all ligand-receptor contacts and the precise ligand-binding mode. From analysis of structural models and mutagenesis, it appears that the position of helices 3, 4 and 5 is crucial in ligand docking. The FFA1-based homology models of FFA2 and FFA3 were constructed and used to compare the FFA subtypes. From docking studies we propose an alternative binding mode for orthosteric agonists at FFA1 and FFA2, involving the interhelical space between helices 4 and 5. This binding mode can explain mutagenesis results for residues at positions 4.56 and 5.42. The novel FFAs structural models highlight higher aromaticity of the FFA2 binding cavity and higher hydrophilicity of the FFA3 binding cavity. The role of the residues at the second extracellular loop used in mutagenesis is reanalysed. The third positively-charged residue in the binding cavity of FFAs, located in helix 2, is identified and predicted to coordinate allosteric modulators.</p><p>The novel structural models of FFAs provide information on specific modes of ligand binding at FFA subtypes and new suggestions for mutagenesis and ligand modification, guiding the development of novel orthosteric and allosteric chemical probes to validate the importance of FFAs in metabolic and inflammatory conditions. Using our FFA homology modelling experience, a strategy to model a GPCR, which is phylogenetically distant from GPCRs with the available crystal structures, is discussed.</p>","PeriodicalId":498,"journal":{"name":"BMC Structural Biology","volume":"15 1","pages":""},"PeriodicalIF":2.222,"publicationDate":"2015-09-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s12900-015-0044-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4319674","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural characterization of the carbohydrate-binding module of NanA sialidase, a pneumococcal virulence factor","authors":"Lei Yang,&nbsp;Helen Connaris,&nbsp;Jane A. Potter,&nbsp;Garry L. Taylor","doi":"10.1186/s12900-015-0042-4","DOIUrl":"https://doi.org/10.1186/s12900-015-0042-4","url":null,"abstract":"<p>\u0000 <i>Streptococcus pneumoniae</i> Neuraminidase A (NanA) is a multi-domain protein anchored to the bacterial surface. Upstream of the catalytic domain of NanA is a domain that conforms to the sialic acid-recognising CBM40 family of the CAZY (carbohydrate-active enzymes) database. This domain has been identified to play a critical role in allowing the bacterium to promote adhesion and invasion of human brain microvascular endothelial cells, and hence may play a key role in promoting bacterial meningitis. In addition, the CBM40 domain has also been reported to activate host chemokines and neutrophil recruitment during infection.</p><p>Crystal structures of both apo- and holo- forms of the NanA CBM40 domain (residues 121 to 305), have been determined to 1.8?? resolution. The domain shares the fold of other CBM40 domains that are associated with sialidases. When in complex with α2,3- or α2,6-sialyllactose, the domain is shown to interact only with the terminal sialic acid. Significantly, a deep acidic pocket adjacent to the sialic acid-binding site is identified, which is occupied by a lysine from a symmetry-related molecule in the crystal. This pocket is adjacent to a region that is predicted to be involved in protein-protein interactions.</p><p>The structural data provide the details of linkage-independent sialyllactose binding by NanA CBM40 and reveal striking surface features that may hold the key to recognition of binding partners on the host cell surface. The structure also suggests that small molecules or sialic acid analogues could be developed to fill the acidic pocket and hence provide a new therapeutic avenue against meningitis caused by <i>S. pneumoniae</i>.</p>","PeriodicalId":498,"journal":{"name":"BMC Structural Biology","volume":"15 1","pages":""},"PeriodicalIF":2.222,"publicationDate":"2015-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s12900-015-0042-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4779248","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Crystal structure of O-methyltransferase CalO6 from the calicheamicin biosynthetic pathway: a case of challenging structure determination at low resolution","authors":"Oleg V. Tsodikov,&nbsp;Caixia Hou,&nbsp;Christopher T. Walsh,&nbsp;Sylvie Garneau-Tsodikova","doi":"10.1186/s12900-015-0040-6","DOIUrl":"https://doi.org/10.1186/s12900-015-0040-6","url":null,"abstract":"<p>Calicheamicins (CAL) are enedyine natural products with potent antibiotic and cytotoxic activity, used in anticancer therapy. The <i>O</i>-methyltransferase CalO6 is proposed to catalyze methylation of the hydroxyl moiety at the C2 position of the orsellinic acid group of CAL.</p><p>Crystals of CalO6 diffracted non-isotropically, with the usable data extending to 3.4??. While no single method of crystal structure determination yielded a structure of CalO6, we were able to determine its structure by using molecular replacement-guided single wavelength anomalous dispersion by using diffraction data from native crystals of CalO6 and a highly non-isomorphous mercury derivative. The structure of CalO6 reveals the methyltransferase fold and dimeric organization characteristic of small molecule <i>O</i>-methyltransferases involved in secondary metabolism in bacteria and plants. Uncommonly, CalO6 was crystallized in the absence of <i>S</i>-adenosylmethionine (SAM; the methyl donor) or <i>S</i>-adenosylhomocysteine (SAH; its product).</p><p>Likely as a consequence of the dynamic nature of CalO6 in the absence of its cofactor, the central region of CalO6, which forms a helical lid-like structure near the active site in CalO6 and similar enzymes, is not observed in the electron density. We propose that this region controls the entry of SAM into and the exit of SAH from the active site of CalO6 and shapes the active site for substrate binding and catalysis.</p>","PeriodicalId":498,"journal":{"name":"BMC Structural Biology","volume":"15 1","pages":""},"PeriodicalIF":2.222,"publicationDate":"2015-07-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s12900-015-0040-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4611760","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structure of the stationary phase survival protein YuiC from B.subtilis","authors":"Doris H.X. Quay,&nbsp;Ambrose R. Cole,&nbsp;Adam Cryar,&nbsp;Konstantinos Thalassinos,&nbsp;Mark A. Williams,&nbsp;Sanjib Bhakta,&nbsp;Nicholas H. Keep","doi":"10.1186/s12900-015-0039-z","DOIUrl":"https://doi.org/10.1186/s12900-015-0039-z","url":null,"abstract":"<p>Stationary phase survival proteins (Sps) were found in Firmicutes as having analogous domain compositions, and in some cases genome context, as the resuscitation promoting factors of Actinobacteria, but with a different putative peptidoglycan cleaving domain.</p><p>The first structure of a Firmicute Sps protein YuiC from <i>B. subtilis</i>, is found to be a stripped down version of the cell-wall peptidoglycan hydrolase MltA. The YuiC structures are of a domain swapped dimer, although some monomer is also found in solution. The protein crystallised in the presence of pentasaccharide shows a 1,6-anhydrodisaccharide sugar product, indicating that YuiC cleaves the sugar backbone to form an anhydro product at least on lengthy incubation during crystallisation.</p><p>The structural simplification of MltA in Sps proteins is analogous to that of the resuscitation promoting factor domains of Actinobacteria, which are stripped down versions of lysozyme and soluble lytic transglycosylase proteins.</p>","PeriodicalId":498,"journal":{"name":"BMC Structural Biology","volume":"15 1","pages":""},"PeriodicalIF":2.222,"publicationDate":"2015-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s12900-015-0039-z","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4456674","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Variations in periplasmic loop interactions determine the pH-dependent activity of the hexameric urea transporter UreI from Helicobacter pylori: a molecular dynamics study","authors":"Javier Cáceres-Delpiano,&nbsp;Jaime Teneb,&nbsp;Rodrigo Mansilla,&nbsp;Apolinaria García,&nbsp;Alexis Salas-Burgos","doi":"10.1186/s12900-015-0038-0","DOIUrl":"https://doi.org/10.1186/s12900-015-0038-0","url":null,"abstract":"<p>\u0000 <i>Helicobacter pylori</i> is an important factor in the development of diseases such as ulcer and gastric cancer. This bacterium uses a periplasmic transporter, UreI, to deliver urea to the intracelullar space, where later it is transformed into ammonia by the cytoplasmic enzyme urease to survive the acidic condition of the human stomach. The UreI transporter presents a pH-dependent activity, where this pH-dependence remains unknown at a structural level. Althought the existance of several protonable residues in the periplasmic loops are related to the pH-dependent activity, we find interesting to have a clear view of the conformational changes involved in this phenomena through a molecular dynamic study.</p><p>Molecular dynamic simulations of the UreI transporter at three different pH conditions were performed, revealing two main pH-dependent conformations, which we present as the open and close states. We find that salt bridges between the periplasmic loops are crucial interactions that stabilize these conformations. Besides, a cooperative behaviour exists between the six subunits of the system that is necessary to fulfill the activity of this transporter.</p><p>We found different pH-dependent conformations of the urea transporter UreI from <i>Helicobacter pylori</i>, which are related to salt-bridge interactions in the periplasmic regions. The behaviour of every channel in the system is not independent, given the existance of a cooperative behaviour through the formation of salt-bridges between the subunits of the hexameric system. We believe that our results will be related to the generation of new eradication therapies using this transporter as an attractive target, denoting that the knowledge of the possible pH-dependent conformations adopted for this transporter are important for the development of rational drug design approximations.</p>","PeriodicalId":498,"journal":{"name":"BMC Structural Biology","volume":"15 1","pages":""},"PeriodicalIF":2.222,"publicationDate":"2015-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s12900-015-0038-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"5009126","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Binding of undamaged double stranded DNA to vaccinia virus uracil-DNA Glycosylase","authors":"Norbert Schormann,&nbsp;Surajit Banerjee,&nbsp;Robert Ricciardi,&nbsp;Debasish Chattopadhyay","doi":"10.1186/s12900-015-0037-1","DOIUrl":"https://doi.org/10.1186/s12900-015-0037-1","url":null,"abstract":"<p>Uracil-DNA glycosylases are evolutionarily conserved DNA repair enzymes. However, vaccinia virus uracil-DNA glycosylase (known as D4), also serves as an intrinsic and essential component of the processive DNA polymerase complex during DNA replication. In this complex D4 binds to a unique poxvirus specific protein A20 which tethers it to the DNA polymerase. At the replication fork the DNA scanning and repair function of D4 is coupled with DNA replication. So far, DNA-binding to D4 has not been structurally characterized.</p><p>This manuscript describes the first structure of a DNA-complex of a uracil-DNA glycosylase from the poxvirus family. This also represents the first structure of a uracil DNA glycosylase in complex with an undamaged DNA. In the asymmetric unit two D4 subunits bind simultaneously to complementary strands of the DNA double helix. Each D4 subunit interacts mainly with the central region of one strand. DNA binds to the opposite side of the A20-binding surface on D4. Comparison of the present structure with the structure of uracil-containing DNA-bound human uracil-DNA glycosylase suggests that for DNA binding and uracil removal D4 employs a unique set of residues and motifs that are highly conserved within the poxvirus family but different in other organisms.</p><p>The first structure of D4 bound to a truly non-specific undamaged double-stranded DNA suggests that initial binding of DNA may involve multiple non-specific interactions between the protein and the phosphate backbone.</p>","PeriodicalId":498,"journal":{"name":"BMC Structural Biology","volume":"15 1","pages":""},"PeriodicalIF":2.222,"publicationDate":"2015-06-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s12900-015-0037-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4431372","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Modeling of the OX1R–orexin-A complex suggests two alternative binding modes","authors":"Lasse Karhu,&nbsp;Ainoleena Turku,&nbsp;Henri Xhaard","doi":"10.1186/s12900-015-0036-2","DOIUrl":"https://doi.org/10.1186/s12900-015-0036-2","url":null,"abstract":"<p>Interactions between the orexin peptides and their cognate OX₁ and OX₂ receptors remain poorly characterized. Site-directed mutagenesis studies on orexin peptides and receptors have indicated amino acids important for ligand binding and receptor activation. However, a better understanding of specific pairwise interactions would benefit small molecule discovery.</p><p>We constructed a set of three-dimensional models of the orexin 1 receptor based on the 3D-structures of the orexin 2 receptor (released while this manuscript was under review), neurotensin receptor 1 and chemokine receptor CXCR4, conducted an exhaustive docking of orexin-A_16–33 peptide fragment with ZDOCK and RDOCK, and analyzed a total of 4301 complexes through multidimensional scaling and clustering. The best docking poses reveal two alternative binding modes, where the C-terminus of the peptide lies deep in the binding pocket, on average about 5–6?? above Tyr^6.48 and close to Gln^3.32. The binding modes differ in the about 100° rotation of the peptide; the peptide His26 faces either the receptor’s fifth transmembrane helix or the seventh helix. Both binding modes are well in line with previous mutation studies and partake in hydrogen bonding similar to suvorexant.</p><p>We present two binding modes for orexin-A into orexin 1 receptor, which help rationalize previous results from site-directed mutagenesis studies. The binding modes should serve small molecule discovery, and offer insights into the mechanism of receptor activation.</p>","PeriodicalId":498,"journal":{"name":"BMC Structural Biology","volume":"15 1","pages":""},"PeriodicalIF":2.222,"publicationDate":"2015-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s12900-015-0036-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4397806","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Human coronavirus OC43 3CL protease and the potential of ML188 as a broad-spectrum lead compound: Homology modelling and molecular dynamic studies","authors":"Michael Berry,&nbsp;Burtram Fielding,&nbsp;Junaid Gamieldien","doi":"10.1186/s12900-015-0035-3","DOIUrl":"https://doi.org/10.1186/s12900-015-0035-3","url":null,"abstract":"<p>The coronavirus 3 chymotrypsin-like protease (3CL^pro) is a validated target in the design of potential anticoronavirus inhibitors. The high degree of homology within the protease’s active site and substrate conservation supports the identification of broad spectrum lead compounds. A previous study identified the compound ML188, also termed 16R, as an inhibitor of the Severe Acute Respiratory Syndrome coronavirus (SARS-CoV) 3CL^pro. This study will detail the generation of a homology model of the 3CL^pro of the human coronavirus OC43 and determine the potential of 16R to form a broad-spectrum lead compound. MODELLER was used to generate a suitable three-dimensional model of the OC43 3CL^pro and the Prime module of Schr?dinger predicted the binding conformation and free energy of binding of 16R within the 3CL^pro active site. Molecular dynamics further confirmed ligand stability and hydrogen bonding networks.</p><p>A high quality homology model of the OC43 3CL^pro was successfully generated in an active conformation. Further studies reproduced the binding pose of 16R within the active site of the generated model, where its free energy of binding was shown to equal that of the 3CL^pro of SARS-CoV, a receptor it is experimentally proven to inhibit. The stability of the ligand was subsequently confirmed by molecular dynamics.</p><p>The lead compound 16R may represent a broad-spectrum inhibitor of the 3CL^pro of OC43 and potentially other coronaviruses. This study provides an atomistic structure of the 3CL^pro of OC43 and supports further experimental validation of the inhibitory effects of 16R. These findings further confirm that the 3CL^pro of coronaviruses can be inhibited by broad spectrum lead compounds.</p>","PeriodicalId":498,"journal":{"name":"BMC Structural Biology","volume":"15 1","pages":""},"PeriodicalIF":2.222,"publicationDate":"2015-04-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s12900-015-0035-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"5516368","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Computational re-engineering of Amylin sequence with reduced amyloidogenic potential","authors":"Mohamed R Smaoui,&nbsp;Jérôme Waldispühl","doi":"10.1186/s12900-015-0034-4","DOIUrl":"https://doi.org/10.1186/s12900-015-0034-4","url":null,"abstract":"<p>The aggregation of amyloid proteins into fibrils is associated with neurodegenerative diseases such as Alzheimer’s and Type II Diabetes. Different methods have explored ways to impede and inhibit amyloid aggregation. Most attempts in the literature involve applying stress to the environment around amyloids. Varying pH levels, modifying temperature, applying pressure through protein crowding and ligand docking are classical examples of these methods. However, environmental stress usually affects molecular pathways and protein functions in the cell and is challenging to construct in vivo. In this paper, we explore destabilizing amyloid proteins through the manipulation of genetic code to create beneficial substitute molecules for patients with certain deficiencies.</p><p>To unravel sequence mutations that destabilize amyloid fibrils yet simultaneously conserve native fold, we analyze the structural landscape of amyloid proteins and search for potential areas that could be exploited to weaken aggregation. Our tool, FibrilMutant, analyzes these regions and studies the effect of amino acid point mutations on nucleation and aggregation. This multiple objective approach impedes aggregation without stressing the cellular environment. We identified six main regions in amyloid proteins that contribute to structural stability and generated amino acid mutations to destabilize those regions. Full length fibrils were built from the mutated amyloid monomers and a dipolar-solvent model capturing the effect of dipole-dipole interactions between water and very large molecular systems to assess their aqueous stability was used to generate energy plots.</p><p>Our results are in agreement with experimental studies and suggest novel targeted single point mutations in the Amylin protein, potentially creating a better therapeutic agent than the currently administered Pramlintide drug for diabetes patients.</p>","PeriodicalId":498,"journal":{"name":"BMC Structural Biology","volume":"15 1","pages":""},"PeriodicalIF":2.222,"publicationDate":"2015-04-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s12900-015-0034-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4914271","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"High-resolution structure of a type IV pilin from the metal-reducing bacterium Shewanella oneidensis","authors":"Manuela Gorgel,&nbsp;Jakob Jensen Ulstrup,&nbsp;Andreas Bøggild,&nbsp;Nykola C Jones,&nbsp;Søren V Hoffmann,&nbsp;Poul Nissen,&nbsp;Thomas Boesen","doi":"10.1186/s12900-015-0031-7","DOIUrl":"https://doi.org/10.1186/s12900-015-0031-7","url":null,"abstract":"<p>Type IV pili are widely expressed among Gram-negative bacteria, where they are involved in biofilm formation, serve in the transfer of DNA, motility and in the bacterial attachment to various surfaces. Type IV pili in <i>Shewanella oneidensis</i> are also supposed to play an important role in extracellular electron transfer by the attachment to sediments containing electron acceptors and potentially forming conductive nanowires.</p><p>The potential nanowire type IV pilin Pil_Bac1 from <i>S. oneidensis</i> was characterized by a combination of complementary structural methods and the atomic structure was determined at a resolution of 1.67?? by X-ray crystallography. Pil_Bac1 consists of one long N-terminal α-helix packed against four antiparallel β-strands, thus revealing the core fold of type IV pilins. In the crystal, Pil_Bac1 forms a parallel dimer with a sodium ion bound to one of the monomers. Interestingly, our Pil_Bac1 crystal structure reveals two unusual features compared to other type IVa pilins: an unusual position of the disulfide bridge and a straight α-helical section, which usually exhibits a pronounced kink. This straight helix leads to a distinct packing in a filament model of Pil_Bac1 based on an EM model of a <i>Neisseria</i> pilus.</p><p>In this study we have described the first structure of a pilin from <i>Shewanella oneidensis</i>. The structure possesses features of the common type IV pilin core, but also exhibits significant variations in the α-helical part and the D-region.</p>","PeriodicalId":498,"journal":{"name":"BMC Structural Biology","volume":"15 1","pages":""},"PeriodicalIF":2.222,"publicationDate":"2015-02-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s12900-015-0031-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"5035355","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}