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Purification, crystallization and preliminary crystallographic analysis of soybean mature glycinin A1bB2. 大豆成熟糖蛋白 A1bB2 的纯化、结晶和初步晶体学分析。
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2013-08-01 Epub Date: 2013-07-27 DOI: 10.1107/S1744309113019684
Krisna Prak, Bunzo Mikami, Takafumi Itoh, Takako Fukuda, Nobuyuki Maruyama, Shigeru Utsumi
{"title":"Purification, crystallization and preliminary crystallographic analysis of soybean mature glycinin A1bB2.","authors":"Krisna Prak, Bunzo Mikami, Takafumi Itoh, Takako Fukuda, Nobuyuki Maruyama, Shigeru Utsumi","doi":"10.1107/S1744309113019684","DOIUrl":"10.1107/S1744309113019684","url":null,"abstract":"<p><p>Glycinin is one of the most abundant storage-protein molecules in soybean seeds and is composed of five subunits (A1aB1b, A1bB2, A2B1a, A3B4 and A5A4B3). A1bB2 was purified from a mutant soybean cultivar containing glycinin composed of only A5A4B3 and A1bB2. At 281 K the protein formed hexagonal, rectangular and rod-shaped crystals in the first [0.1 M imidazole pH 8.0, 0.2 M MgCl₂, 35%(v/v) MPD], second [0.1 M sodium citrate pH 5.6, 0.2 M ammonium acetate, 30%(v/v) MPD] and third (0.1 M phosphate-citrate pH 4.2, 2.0 M ammonium sulfate) crystallization conditions, respectively. X-ray diffraction data were collected to resolutions of 1.85, 1.85 and 2.5 Å from crystals of the three different shapes. The crystals belonged to space groups P6₃22, P2₁ and P1, with unit-cell parameters a = b = 143.60, c = 84.54 Å, a = 114.54, b = 105.82, c = 116.67 Å, β = 94.99° and a = 94.45, b = 94.96, c = 100.66 Å, α = 107.02, β = 108.44, γ = 110.71°, respectively. One, six and six subunits of A1bB2 were estimated to be present in the respective asymmetric units. The three-dimensional structure of the A1bB2 hexamer is currently being determined.</p>","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":"69 Pt 8","pages":"937-41"},"PeriodicalIF":0.9,"publicationDate":"2013-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3729179/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31625484","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Acta Crystallographica Section F: Structural Biology Communications. Acta Crystallographica Section F: Structural Biology Communications.
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2013-08-01 Epub Date: 2013-07-30 DOI: 10.1107/S1744309113020873
Howard Einspahr, Manfred S Weiss
{"title":"Acta Crystallographica Section F: Structural Biology Communications.","authors":"Howard Einspahr, Manfred S Weiss","doi":"10.1107/S1744309113020873","DOIUrl":"10.1107/S1744309113020873","url":null,"abstract":"","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":"69 Pt 8","pages":"827"},"PeriodicalIF":0.9,"publicationDate":"2013-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3729152/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31626195","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
The future of crystallization communications in Acta Cryst. F. 晶体学报中结晶通讯的未来。F。
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2013-07-01 Epub Date: 2013-06-30 DOI: 10.1107/S1744309113017909
Manfred S Weiss, Howard Einspahr
{"title":"The future of crystallization communications in Acta Cryst. F.","authors":"Manfred S Weiss,&nbsp;Howard Einspahr","doi":"10.1107/S1744309113017909","DOIUrl":"https://doi.org/10.1107/S1744309113017909","url":null,"abstract":"Editorial.","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":"69 Pt 7","pages":"711"},"PeriodicalIF":0.9,"publicationDate":"2013-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1744309113017909","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31203170","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 2
X-ray diffraction studies on merohedrally twinned Δ1-62NtNBCe1-A crystals of the sodium/bicarbonate cotransporter. 对钠离子/碳酸氢盐共转运体的Δ1-62NtNBCe1-A 晶体的 X 射线衍射研究。
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2013-07-01 Epub Date: 2013-06-28 DOI: 10.1107/S1744309113016710
Harindarpal S Gill, Lauren Dutcher, Walter F Boron, Samir Patel, Lisa M Guay-Woodford
{"title":"X-ray diffraction studies on merohedrally twinned Δ1-62NtNBCe1-A crystals of the sodium/bicarbonate cotransporter.","authors":"Harindarpal S Gill, Lauren Dutcher, Walter F Boron, Samir Patel, Lisa M Guay-Woodford","doi":"10.1107/S1744309113016710","DOIUrl":"10.1107/S1744309113016710","url":null,"abstract":"<p><p>NBCe1-A membrane-embedded macromolecules that cotransport sodium and bicarbonate ions across the bilayer serve to maintain acid-base homeostasis throughout the body. Defects result in a number of renal and eye disorders, including type-II renal tubular acidosis and cataracts. Here, crystals of a human truncated mutant of the cytoplasmic N-terminal domain of NBCe1 (Δ1-62NtNBCe1-A) are reported that diffract X-rays to 2.4 Å resolution. The crystal symmetry of Δ1-62NtNBCe1-A is of space group P31 with pseudo-P3121 symmetry and it has a hemihedral twin fraction of 33.0%. The crystals may provide insight into the pathogenic processes observed in a subset of patients with truncating and point mutations in the gene encoding NBCe1.</p>","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":"69 Pt 7","pages":"796-9"},"PeriodicalIF":0.9,"publicationDate":"2013-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3702328/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31561524","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
ErpC, a member of the complement regulator-acquiring family of surface proteins from Borrelia burgdorferi, possesses an architecture previously unseen in this protein family. ErpC是伯氏疏螺旋体表面蛋白补体调控获得家族的一员，具有以前在该蛋白家族中未见的结构。
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2013-06-01 Epub Date: 2013-05-23 DOI: 10.1107/S1744309113013249
Joseph J E Caesar, Steven Johnson, Peter Kraiczy, Susan M Lea
{"title":"ErpC, a member of the complement regulator-acquiring family of surface proteins from Borrelia burgdorferi, possesses an architecture previously unseen in this protein family.","authors":"Joseph J E Caesar,&nbsp;Steven Johnson,&nbsp;Peter Kraiczy,&nbsp;Susan M Lea","doi":"10.1107/S1744309113013249","DOIUrl":"10.1107/S1744309113013249","url":null,"abstract":"<p><p>Borrelia burgdorferi is a spirochete responsible for Lyme disease, the most commonly occurring vector-borne disease in Europe and North America. The bacterium utilizes a set of proteins, termed complement regulator-acquiring surface proteins (CRASPs), to aid evasion of the human complement system by recruiting and presenting complement regulator factor H on its surface in a manner that mimics host cells. Presented here is the atomic resolution structure of a member of this protein family, ErpC. The structure provides new insights into the mechanism of recruitment of factor H and other factor H-related proteins by acting as a molecular mimic of host glycosaminoglycans. It also describes the architecture of other CRASP proteins belonging to the OspE/F-related paralogous protein family and suggests that they have evolved to bind specific complement proteins, aiding survival of the bacterium in different hosts.</p>","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":"69 Pt 6","pages":"624-8"},"PeriodicalIF":0.9,"publicationDate":"2013-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1744309113013249","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31470678","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 13
Structure of PatF from Prochloron didemni. Prochloron didemni 的 PatF 结构。
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2013-06-01 Epub Date: 2013-05-23 DOI: 10.1107/S1744309113012931
Andrew F Bent, Jesko Koehnke, Wael E Houssen, Margaret C M Smith, Marcel Jaspars, James H Naismith
{"title":"Structure of PatF from Prochloron didemni.","authors":"Andrew F Bent, Jesko Koehnke, Wael E Houssen, Margaret C M Smith, Marcel Jaspars, James H Naismith","doi":"10.1107/S1744309113012931","DOIUrl":"10.1107/S1744309113012931","url":null,"abstract":"<p><p>Patellamides are macrocyclic peptides with potent biological effects and are a subset of the cyanobactins. Cyanobactins are natural products that are produced by a series of enzymatic transformations and a common modification is the addition of a prenyl group. Puzzlingly, the pathway for patellamides in Prochloron didemni contains a gene, patF, with homology to prenylases, but patellamides are not themselves prenylated. The structure of the protein PatF was cloned, expressed, purified and determined. Prenylase activity could not be demonstrated for the protein, and examination of the structure revealed changes in side-chain identity at the active site. It is suggested that these changes have inactivated the protein. Attempts to mutate these residues led to unfolded protein.</p>","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":"69 Pt 6","pages":"618-23"},"PeriodicalIF":0.9,"publicationDate":"2013-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3668578/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31470181","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Structure of diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase from Acinetobacter baumannii. 鲍曼不动杆菌中的二氨基羟基磷酸核糖基氨基嘧啶脱氨酶/5-氨基-6-（5-磷酸核糖基氨基）尿嘧啶还原酶的结构。
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2013-06-01 Epub Date: 2013-05-23 DOI: 10.1107/S174430911301292X
Alice Dawson, Paul Trumper, Georgios Chrysostomou, William N Hunter
{"title":"Structure of diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase from Acinetobacter baumannii.","authors":"Alice Dawson, Paul Trumper, Georgios Chrysostomou, William N Hunter","doi":"10.1107/S174430911301292X","DOIUrl":"10.1107/S174430911301292X","url":null,"abstract":"<p><p>The bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase (RibD) represents a potential antibacterial drug target. The structure of recombinant Acinetobacter baumannii RibD is reported in orthorhombic and tetragonal crystal forms at 2.2 and 2.0 Å resolution, respectively. Comparisons with orthologous structures in the Protein Data Bank indicated close similarities. The tetragonal crystal form was obtained in the presence of guanosine monophosphate, which surprisingly was observed to occupy the adenine-binding site of the reductase domain.</p>","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":"69 Pt 6","pages":"611-7"},"PeriodicalIF":0.9,"publicationDate":"2013-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3668577/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31470180","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Further structural insights into the binding of complement factor H by complement regulator-acquiring surface protein 1 (CspA) of Borrelia burgdorferi. 从结构上进一步了解包虫病补体调节剂获取表面蛋白 1（CspA）与补体因子 H 的结合。
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2013-06-01 Epub Date: 2013-05-23 DOI: 10.1107/S1744309113012748
Joseph J E Caesar, Reinhard Wallich, Peter Kraiczy, Peter F Zipfel, Susan M Lea
{"title":"Further structural insights into the binding of complement factor H by complement regulator-acquiring surface protein 1 (CspA) of Borrelia burgdorferi.","authors":"Joseph J E Caesar, Reinhard Wallich, Peter Kraiczy, Peter F Zipfel, Susan M Lea","doi":"10.1107/S1744309113012748","DOIUrl":"10.1107/S1744309113012748","url":null,"abstract":"<p><p>Borrelia burgdorferi has evolved many mechanisms of evading the different immune systems across its range of reservoir hosts, including the capture and presentation of host complement regulators factor H and factor H-like protein-1 (FHL-1). Acquisition is mediated by a family of complement regulator-acquiring surface proteins (CRASPs), of which the atomic structure of CspA (BbCRASP-1) is known and shows the formation of a homodimeric species which is required for binding. Mutagenesis studies have mapped a putative factor H binding site to a cleft between the two subunits. Presented here is a new atomic structure of CspA which shows a degree of flexibility between the subunits which may be critical for factor H scavenging by increasing access to the binding interface and allows the possibility that the assembly can clamp around the bound complement regulators.</p>","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":"69 Pt 6","pages":"629-33"},"PeriodicalIF":0.9,"publicationDate":"2013-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3668580/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31470182","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Deer mouse hemoglobin exhibits a lowered oxygen affinity owing to mobility of the E helix. Corrigendum 鹿鼠血红蛋白由于E螺旋的移动而表现出较低的氧亲和力。应改正的错误
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2013-05-29 DOI: 10.1107/S1744309113011093
N. Inoguchi, Jake R. Oshlo, Chandrasekhar Natarajan, R. Weber, A. Fago, J. F. Storz, H. Moriyama
{"title":"Deer mouse hemoglobin exhibits a lowered oxygen affinity owing to mobility of the E helix. Corrigendum","authors":"N. Inoguchi, Jake R. Oshlo, Chandrasekhar Natarajan, R. Weber, A. Fago, J. F. Storz, H. Moriyama","doi":"10.1107/S1744309113011093","DOIUrl":"https://doi.org/10.1107/S1744309113011093","url":null,"abstract":"A corrigendum to the article by Inoguchi et al. [(2013). Acta Cryst. F69, 393–398].","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":"101-B 9 1","pages":"710 - 710"},"PeriodicalIF":0.9,"publicationDate":"2013-05-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74686979","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Structure of the hypothetical DUF1811-family protein GK0453 from Geobacillus kaustophilus HTA426. 来自高嗜地气杆菌 HTA426 的假想 DUF1811 家族蛋白 GK0453 的结构。
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2013-04-01 Epub Date: 2013-03-28 DOI: 10.1107/S1744309113003369
Balasundaram Padmanabhan, Yoshihiro Nakamura, Svetlana V Antonyuk, Richard W Strange, S Samar Hasnain, Shigeyuki Yokoyama, Yoshitaka Bessho
{"title":"Structure of the hypothetical DUF1811-family protein GK0453 from Geobacillus kaustophilus HTA426.","authors":"Balasundaram Padmanabhan, Yoshihiro Nakamura, Svetlana V Antonyuk, Richard W Strange, S Samar Hasnain, Shigeyuki Yokoyama, Yoshitaka Bessho","doi":"10.1107/S1744309113003369","DOIUrl":"10.1107/S1744309113003369","url":null,"abstract":"<p><p>The crystal structure of a conserved hypothetical protein, GK0453, from Geobacillus kaustophilus has been determined to 2.2 Å resolution. The crystal belonged to space group P4(3)2(1)2, with unit-cell parameters a = b = 75.69, c = 64.18 Å. The structure was determined by the molecular-replacement method and was refined to a final R factor of 22.6% (R(free) = 26.3%). Based on structural homology, the GK0453 protein possesses two independent binding sites and hence it may simultaneously interact with two proteins or with a protein and a nucleic acid.</p>","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":"69 Pt 4","pages":"342-5"},"PeriodicalIF":0.9,"publicationDate":"2013-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3614154/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40240964","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
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