Journal of Structural Biology: X最新文献

{"title":"Current view of iron biomineralization in magnetotactic bacteria","authors":"Shirel Ben-Shimon ,&nbsp;Daniel Stein ,&nbsp;Raz Zarivach","doi":"10.1016/j.yjsbx.2021.100052","DOIUrl":"10.1016/j.yjsbx.2021.100052","url":null,"abstract":"<div><p>Biomineralization is the process of mineral formation by living organisms. One notable example of these organisms is magnetotactic bacteria (MTB). MTB are Gram-negative bacteria that can biomineralize iron into magnetic nanoparticles. This ability allows these aquatic microorganisms to orient themselves according to the geomagnetic field. The biomineralization process takes place in a specialized sub-cellular membranous organelle, the magnetosome. The magnetosome contains a defined set of magnetosome-associated proteins (MAPs) that controls the biomineralization environment, including iron concentration, redox, and pH. Magnetite formation is subjected to a tight regulation within the magnetosome that affects the nanoparticle nucleation, size, and shape, leading to well-defined magnetic properties. The formed magnetite nanoparticles have unique characteristics of a stable, single magnetic domain with narrow size distribution and high crystalline structures, which turned MTB into the subject of interest in multidisciplinary research. This graphical review provides a current overview of iron biomineralization in magnetotactic bacteria, focusing on Alphaproteobacteria. To better understand this complex mechanism, we present the four main steps and the main MAPs participating in the process of magnetosome formation.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"5 ","pages":"Article 100052"},"PeriodicalIF":2.9,"publicationDate":"2021-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/b8/9e/main.PMC8536778.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39669152","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 a homotrimeric verrucomicrobial exo-β-1,4-mannosidase active in the hindgut of the wood-feeding termite Reticulitermes flavipes","authors":"Dayanand C. Kalyani ,&nbsp;Tom Reichenbach ,&nbsp;Markus M. Keskitalo ,&nbsp;Julian Conrad ,&nbsp;Henrik Aspeborg ,&nbsp;Christina Divne","doi":"10.1016/j.yjsbx.2021.100048","DOIUrl":"https://doi.org/10.1016/j.yjsbx.2021.100048","url":null,"abstract":"<div><p>The termite <em>Reticulitermes flavipes</em> causes extensive damage due to the high efficiency and broad specificity of the ligno- and hemicellulolytic enzyme systems produced by its symbionts. Thus, the <em>R. flavipes</em> gut microbiome is expected to constitute an excellent source of enzymes that can be used for the degradation and valorization of plant biomass. The symbiont <em>Opitutaceae</em> bacterium strain TAV5 belongs to the phylum Verrucomicrobia and thrives in the hindgut of <em>R. flavipes</em>. The sequence of the gene with the locus tag opit5_10225 in the <em>Opitutaceae</em> bacterium strain TAV5 genome has been classified as a member of glycoside hydrolase family 5 (GH5), and provisionally annotated as an <em>endo</em>-<em>β</em>-mannanase. We characterized biochemically and structurally the opit5_10225 gene product, and show that the enzyme, <em>Op5</em>Man5, is an <em>exo</em>-<em>β</em>-1,4-mannosidase [EC 3.2.1.25] that is highly specific for <em>β</em>-1,4-mannosidic bonds in mannooligosaccharides and ivory nut mannan. The structure of <em>Op5</em>Man5 was phased using electron cryo-microscopy and further determined and refined at 2.2 Å resolution using X-ray crystallography. <em>Op5</em>Man5 features a 200-kDa large homotrimer composed of three modular monomers. Despite insignificant sequence similarity, the structure of the monomer, and homotrimeric assembly are similar to that of the GH42-family <em>β</em>-galactosidases and the GH164-family <em>exo</em>-<em>β</em>-1,4-mannosidase <em>Bs</em>164 from <em>Bacteroides salyersiae</em>. To the best of our knowledge <em>Op5</em>Man5 is the first structure of a glycoside hydrolase from a bacterial symbiont isolated from the <em>R. flavipes</em> digestive tract, as well as the first example of a GH5 glycoside hydrolase with a GH42 <em>β</em>-galactosidase-type homotrimeric structure.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"5 ","pages":"Article 100048"},"PeriodicalIF":2.9,"publicationDate":"2021-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2021.100048","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72075949","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":"Cyclodextrins for structural and functional studies of mechanosensitive channels","authors":"Yixiao Zhang ,&nbsp;Gabriella Angiulli ,&nbsp;Boris Martinac ,&nbsp;Charles D. Cox ,&nbsp;Thomas Walz","doi":"10.1016/j.yjsbx.2021.100053","DOIUrl":"10.1016/j.yjsbx.2021.100053","url":null,"abstract":"<div><p>Mechanosensitive (MS) channels that are activated by the ‘force-from-lipids’ (FFL) principle rest in the membrane in a closed state but open a transmembrane pore in response to changes in the transmembrane pressure profile. The molecular implementations of the FFL principle vary widely between different MS channel families. The function of MS channels is often studied by patch-clamp electrophysiology, in which mechanical force or amphipathic molecules are used to activate the channels. Structural studies of MS channels in states other than the closed resting state typically relied on the use of mutant channels. Cyclodextrins (CDs) were recently introduced as a relatively easy and convenient approach to generate membrane tension. The principle is that CDs chelate hydrophobic molecules and can remove lipids from membranes, thus forcing the remaining lipids to cover more surface area and creating tension for membrane proteins residing in the membranes. CDs can be used to study the structure of MS channels in a membrane under tension by using single-particle cryo-electron microscopy to image the channels in nanodiscs after incubation with CDs as well as to characterize the function of MS channels by using patch-clamp electrophysiology to record the effect of CDs on channels inserted into membrane patches excised from proteoliposomes. Importantly, because incubation of membrane patches with CDs results in the activation of MscL, an MS channel that opens only shortly before membrane rupture, CD-mediated lipid removal appears to generate sufficient force to open most if not all types of MS channels that follow the FFL principle.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"5 ","pages":"Article 100053"},"PeriodicalIF":2.9,"publicationDate":"2021-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8593449/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39906423","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 and intermolecular interactions in spheroidal high-density lipoprotein subpopulations","authors":"Chris J. Malajczuk ,&nbsp;Neha S. Gandhi ,&nbsp;Ricardo L. Mancera","doi":"10.1016/j.yjsbx.2020.100042","DOIUrl":"10.1016/j.yjsbx.2020.100042","url":null,"abstract":"<div><p>Human serum high-density lipoproteins (HDLs) are a population of small, dense protein-lipid aggregates that are crucial for intravascular lipid trafficking and are protective against cardiovascular disease. The spheroidal HDL subfraction can be separated by size and density into five major subpopulations with distinct molecular compositions and unique biological functionalities: HDL_3c, HDL_3b, HDL_3a, HDL_2a and HDL_2b. Representative molecular models of these five subpopulations were developed and characterised for the first time in the presence of multiple copies of its primary protein component apolipoprotein A-I (apoA-I) using coarse-grained molecular dynamics simulations. Each HDL model exhibited size, morphological and compositional profiles consistent with experimental observables. With increasing particle size the separation of core and surface molecules became progressively more defined, resulting in enhanced core lipid mixing, reduced core lipid exposure at the surface, and the formation of an interstitial region between core and surface molecules in HDL_2b. Cholesterol molecules tended to localise around the central helix-5 of apoA-I, whilst triglyceride molecules predominantly interacted with aromatic, hydrophobic residues located within the terminal helix-10 across all subpopulation models. The three intermediate HDL models exhibited similar surface profiles despite having distinct molecular compositions. ApoA-I in trefoil, quatrefoil and pentafoil arrangements across the surface of HDL particles exhibited significant warping and twisting, but largely retained intermolecular contacts between adjacent apoA-I chains. Representative HDL subpopulations differed in particle size, morphology, intermolecular interaction profiles and lipid and protein dynamics. These findings reveal how different HDL subpopulations might exhibit distinct functional associations depending on particle size, form and composition.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"5 ","pages":"Article 100042"},"PeriodicalIF":2.9,"publicationDate":"2021-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2020.100042","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38814565","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":"Systematized analysis of secondary structure dependence of key structural features of residues in soluble and membrane-bound proteins","authors":"Mohammed H. AL Mughram ,&nbsp;Noah B. Herrington ,&nbsp;Claudio Catalano ,&nbsp;Glen E. Kellogg","doi":"10.1016/j.yjsbx.2021.100055","DOIUrl":"10.1016/j.yjsbx.2021.100055","url":null,"abstract":"<div><p>Knowledge of three-dimensional protein structure is integral to most modern drug discovery efforts. Recent advancements have highlighted new techniques for 3D protein structure determination and, where structural data cannot be collected experimentally, prediction of protein structure. We have undertaken a major effort to use existing protein structures to collect, characterize, and catalogue the inter-atomic interactions that define and compose 3D structure by mapping hydropathic interaction environments as maps in 3D space. This work has been performed on a residue-by-residue basis, where we have seen evidence for relationships between environment character, residue solvent-accessible surface areas and their secondary structures. In this graphical review, we apply principles from our earlier studies and expand the scope to all common amino acid residue types in both soluble and membrane proteins. Key to this analysis is parsing the Ramachandran plot to an 8-by-8 chessboard to define secondary structure bins. Our analysis yielded a number of quantitative discoveries: 1) increased fraction of hydrophobic residues (alanine, isoleucine, leucine, phenylalanine and valine) in membrane proteins compared to their fractions in soluble proteins; 2) less burial coupled with significant increases in favorable hydrophobic interactions for hydrophobic residues in membrane proteins compared to soluble proteins; and 3) higher burial and more favorable polar interactions for polar residues now preferring the interior of membrane proteins. These observations and the supporting data should provide benchmarks for current studies of protein residues in different environments and may be able to guide future protein structure prediction efforts.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"5 ","pages":"Article 100055"},"PeriodicalIF":2.9,"publicationDate":"2021-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/33/90/main.PMC8654985.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39746717","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 flexibility of the tetanus neurotoxin revealed by crystallographic and solution scattering analyses","authors":"Chun-ming Zhang ,&nbsp;Yoshihiro Imoto ,&nbsp;Takaaki Hikima ,&nbsp;Tsuyoshi Inoue","doi":"10.1016/j.yjsbx.2021.100045","DOIUrl":"10.1016/j.yjsbx.2021.100045","url":null,"abstract":"<div><p>Although the tetanus neurotoxin (TeNT) delivers its protease domain (LC) across the synaptic vesicle lumen into the cytosol via its receptor binding domain (H_C) and translocation domain (H_N), the molecular mechanism coordinating this membrane translocation remains unresolved. Here, we report the high-resolution crystal structures of full-length reduced TeNT (rTeNT, 2.3 Å), TeNT isolated H_N (TeNT/iH_N, 2.3 Å), TeNT isolated H_C (TeNT/iH_C, 1.5 Å), together with the solution structures of TeNT/iH_N and beltless TeNT/iH_N (TeNT/blH_N). TeNT undergoes significant domains rotation of the H_N and LC were demonstrated by structural comparison of rTeNT and non-reduced-TeNT (nrTeNT). A linker loop connects the H_N and H_C is essential for the self-domain rotation of TeNT. The TeNT-specific C869-C1093 disulfide bond is sensitive to the redox environment and its disruption provides linker loop flexibility, which enables domain arrangement of rTeNT distinct from that of nrTeNT. Furthermore, the mobility of C869 in the linker loop and the sensitivity to redox condition of C1093 were confirmed by crystal structure analysis of TeNT/iH_C. On the other hand, the structural flexibility of H_N was investigated by crystallographic and solution scattering analyses. It was found that the region (residues 698–769), which follows the translocation region had remarkable change in TeNT/iH_N. Besides, the so-called belt region has a high propensity to swing around the upper half of TeNT/iH_N at acidic pH. It provides the first overview of the dynamics of the Belt in solution. These newly obtained structural information that shed light on the transmembrane mechanism of TeNT.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"5 ","pages":"Article 100045"},"PeriodicalIF":2.9,"publicationDate":"2021-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2021.100045","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25378915","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":"The structure of the cysteine-rich region from human histone-lysine N-methyltransferase EHMT2 (G9a)","authors":"Keshia M. Kerchner ,&nbsp;Tung-Chung Mou ,&nbsp;Yizhi Sun ,&nbsp;Domniţa-Valeria Rusnac ,&nbsp;Stephen R. Sprang ,&nbsp;Klára Briknarová","doi":"10.1016/j.yjsbx.2021.100050","DOIUrl":"10.1016/j.yjsbx.2021.100050","url":null,"abstract":"<div><p>Euchromatic histone-lysine N-methyltransferase 1 (EHMT1; G9a-like protein; GLP) and euchromatic histone-lysine N-methyltransferase 2 (EHMT2; G9a) are protein lysine methyltransferases that regulate gene expression and are essential for development and the ability of organisms to change and adapt. In addition to ankyrin repeats and the catalytic SET domain, the EHMT proteins contain a unique cysteine-rich region (CRR) that mediates protein–protein interactions and recruitment of the methyltransferases to specific sites in chromatin. We have determined the structure of the CRR from human EHMT2 by X-ray crystallography and show that the CRR adopts an unusual compact fold with four bound zinc atoms. The structure consists of a RING domain preceded by a smaller zinc-binding motif and an N-terminal segment. The smaller zinc-binding motif straddles the N-terminal end of the RING domain, and the N-terminal segment runs in an extended conformation along one side of the structure and interacts with both the smaller zinc-binding motif and the RING domain. The interface between the N-terminal segment and the RING domain includes one of the zinc atoms. The RING domain is partially sequestered within the CRR and unlikely to function as a ubiquitin ligase.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"5 ","pages":"Article 100050"},"PeriodicalIF":2.9,"publicationDate":"2021-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2021.100050","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39197180","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 two solute-binding proteins for N,N′-diacetylchitobiose/N,N′,N′′-triacetylchitotoriose of the gram-positive bacterium, Paenibacillus sp. str. FPU-7","authors":"Takafumi Itoh,&nbsp;Misaki Yaguchi,&nbsp;Akari Nakaichi,&nbsp;Moe Yoda,&nbsp;Takao Hibi,&nbsp;Hisashi Kimoto","doi":"10.1016/j.yjsbx.2021.100049","DOIUrl":"https://doi.org/10.1016/j.yjsbx.2021.100049","url":null,"abstract":"<div><p>The chitinolytic bacterium <em>Paenibacillus</em> sp. str. FPU-7 efficiently degrades chitin into oligosaccharides such as <em>N</em>-acetyl-D-glucosamine (GlcNAc) and disaccharides (GlcNAc)₂ through multiple secretory chitinases. Transport of these oligosaccharides by <em>P</em>. str. FPU-7 has not yet been clarified. In this study, we identified <em>nagB1</em>, predicted to encode a sugar solute-binding protein (SBP), which is a component of the ABC transport system. However, the genes next to <em>nagB1</em> were predicted to encode two-component regulatory system proteins rather than transmembrane domains (TMDs). We also identified <em>nagB2</em>, which is highly homologous to <em>nagB1</em>. Adjacent to <em>nagB2</em>, two genes were predicted to encode TMDs. Binding experiments of the recombinant NagB1 and NagB2 to several oligosaccharides using differential scanning fluorimetry and surface plasmon resonance confirmed that both proteins are SBPs of (GlcNAc)₂ and (GlcNAc)₃. We determined their crystal structures complexed with and without chitin oligosaccharides at a resolution of 1.2 to 2.0 Å. The structures shared typical SBP structural folds and were classified as subcluster D-I. Large domain motions were observed in the structures, suggesting that they were induced by ligand binding via the “Venus flytrap” mechanism. These structures also revealed chitin oligosaccharide recognition mechanisms. In conclusion, our study provides insight into the recognition and transport of chitin oligosaccharides in bacteria.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"5 ","pages":"Article 100049"},"PeriodicalIF":2.9,"publicationDate":"2021-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2021.100049","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72114796","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 analysis of missense mutations occurring in the DNA-binding domain of HSF4 associated with congenital cataracts","authors":"Zaiyu Xiao ,&nbsp;Ling Guo ,&nbsp;Yang Zhang ,&nbsp;Liwei Cui ,&nbsp;Yujie Dai ,&nbsp;Zhu Lan ,&nbsp;Qinghua Zhang ,&nbsp;Sheng Wang ,&nbsp;Wei Liu","doi":"10.1016/j.yjsbx.2019.100015","DOIUrl":"10.1016/j.yjsbx.2019.100015","url":null,"abstract":"<div><p>Congenital cataract (CC) is the major cause of childish blindness, and nearly 50% of CCs are hereditary disorders. HSF4, a member of the heat shock transcription factor family, acts as a key regulator of cell growth and differentiation during the development of sensory organs. Missense mutations in the HSF4-encoding gene have been reported to cause CC formation; in particular, those occurring within the DNA-binding domain (DBD) are usually autosomal dominant mutations. To address how the identified mutations lead to HSF4 malfunction by placing adverse impacts on protein structure and DNA-binding specificity and affinity, we determined two high-resolution structures of the wild-type DBD and the K23N mutant of human HSF4, built DNA-binding models, conducted <em>in silico</em> mutations and molecular dynamics simulations. Our analysis suggests four possible structural mechanisms underlining the missense mutations in HSF4-DBD and cataractogenesis: (i), disruption of HSE recognition; (ii), perturbation of protein-DNA interactions; (iii), alteration of protein folding; (iv), other impacts, e.g. inhibition of protein oligomerization.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"4 ","pages":"Article 100015"},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2019.100015","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38137263","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":"FMN riboswitch aptamer symmetry facilitates conformational switching through mutually exclusive coaxial stacking configurations","authors":"Haley M. Wilt ,&nbsp;Ping Yu ,&nbsp;Kemin Tan ,&nbsp;Yun-Xing Wang ,&nbsp;Jason R. Stagno","doi":"10.1016/j.yjsbx.2020.100035","DOIUrl":"10.1016/j.yjsbx.2020.100035","url":null,"abstract":"<div><p>Knowledge of both apo and holo states of riboswitches aid in elucidating the various mechanisms of ligand-induced conformational “switching” that underpin their gene-regulating capabilities. Previous structural studies on the flavin mononucleotide (FMN)-binding aptamer of the FMN riboswitch, however, have revealed minimal conformational changes associated with ligand binding that do not adequately explain the basis for the switching behavior. We have determined a 2.7-Å resolution crystal structure of the ligand-free FMN riboswitch aptamer that is distinct from previously reported structures, particularly in the conformation and orientation of the P1 and P4 helices. The nearly symmetrical tertiary structure provides a mechanism by which one of two pairs of adjacent helices (P3/P4 or P1/P6) undergo collinear stacking in a mutually exclusive manner, in the absence or presence of ligand, respectively. Comparison of these structures suggests the stem-loop that includes P4 and L4 is important for maintaining a global conformational state that, in the absence of ligand, disfavors formation of the P1 regulatory helix. Together, these results provide further insight to the structural basis for conformational switching of the FMN riboswitch.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"4 ","pages":"Article 100035"},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2020.100035","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38529452","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}