Acta Crystallographica Section F-structural Biology and Crystallization Communications最新文献_第6页

ATP-dependent DNA ligase from Thermococcus sp. 1519 displays a new arrangement of the OB-fold domain. 来自热球菌sp. 1519的atp依赖性DNA连接酶显示了OB-fold结构域的新排列。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-12-01 Epub Date: 2012-11-14 DOI: 10.1107/S1744309112043394

T Petrova, E Y Bezsudnova, K M Boyko, A V Mardanov, K M Polyakov, V V Volkov, M Kozin, N V Ravin, I G Shabalin, K G Skryabin, T N Stekhanova, M V Kovalchuk, V O Popov

{"title":"ATP-dependent DNA ligase from Thermococcus sp. 1519 displays a new arrangement of the OB-fold domain.","authors":"T Petrova, E Y Bezsudnova, K M Boyko, A V Mardanov, K M Polyakov, V V Volkov, M Kozin, N V Ravin, I G Shabalin, K G Skryabin, T N Stekhanova, M V Kovalchuk, V O Popov","doi":"10.1107/S1744309112043394","DOIUrl":"10.1107/S1744309112043394","url":null,"abstract":"DNA ligases join single-strand breaks in double-stranded DNA by catalyzing the formation of a phosphodiester bond between adjacent 5'-phosphate and 3'-hydroxyl termini. Their function is essential for maintaining genome integrity in the replication, recombination and repair of DNA. High flexibility is important for the function of DNA ligase molecules. Two types of overall conformations of archaeal DNA ligase that depend on the relative position of the OB-fold domain have previously been revealed: closed and open extended conformations. The structure of ATP-dependent DNA ligase from Thermococcus sp. 1519 (LigTh1519) in the crystalline state determined at a resolution of 3.02 Å shows a new relative arrangement of the OB-fold domain which is intermediate between the positions of this domain in the closed and the open extended conformations of previously determined archaeal DNA ligases. However, small-angle X-ray scattering (SAXS) measurements indicate that in solution the LigTh1519 molecule adopts either an open extended conformation or both an intermediate and an open extended conformation with the open extended conformation being dominant.","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":"68 Pt 12","pages":"1440-7"},"PeriodicalIF":0.9,"publicationDate":"2012-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1744309112043394","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31081138","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: 15

Crystallization of domains involved in self-assembly of the S-layer protein SbsC. s层蛋白SbsC自组装结构域的结晶。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-12-01 Epub Date: 2012-11-14 DOI: 10.1107/S1744309112042650

Anđela Ðordić, Eva M Egelseer, Manfred Tesarz, Uwe B Sleytr, Walter Keller, Tea Pavkov-Keller

引用次数: 8

Recombinant production, crystallization and X-ray crystallographic structure determination of the peptidyl-tRNA hydrolase of Pseudomonas aeruginosa. 铜绿假单胞菌肽基-tRNA水解酶的重组生产、结晶和 X 射线晶体学结构测定。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-12-01 Epub Date: 2012-11-28 DOI: 10.1107/S1744309112045770

Ronny C Hughes, Hana McFeeters, Leighton Coates, Robert L McFeeters

{"title":"Recombinant production, crystallization and X-ray crystallographic structure determination of the peptidyl-tRNA hydrolase of Pseudomonas aeruginosa.","authors":"Ronny C Hughes, Hana McFeeters, Leighton Coates, Robert L McFeeters","doi":"10.1107/S1744309112045770","DOIUrl":"10.1107/S1744309112045770","url":null,"abstract":"The peptidyl-tRNA hydrolase enzyme from the pathogenic bacterium Pseudomonas aeruginosa (Pth; EC 3.1.1.29) has been cloned, expressed in Escherichia coli and crystallized for X-ray structural analysis. Suitable crystals were grown using the sitting-drop vapour-diffusion method after one week of incubation against a reservoir solution consisting of 20% polyethylene glycol 4000, 100 mM Tris pH 7.5, 10%(v/v) isopropyl alcohol. The crystals were used to obtain the three-dimensional structure of the native protein at 1.77 Å resolution. The structure was determined by molecular replacement of the crystallographic data processed in space group P6(1)22 with unit-cell parameters a=b=63.62, c=155.20 Å, α=β=90, γ=120°. The asymmetric unit of the crystallographic lattice was composed of a single copy of the enzyme molecule with a 43% solvent fraction, corresponding to a Matthews coefficient of 2.43 Å3 Da(-1). The crystallographic structure reported here will serve as the foundation for future structure-guided efforts towards the development of novel small-molecule inhibitors specific to bacterial Pths.","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":"68 Pt 12","pages":"1472-6"},"PeriodicalIF":0.9,"publicationDate":"2012-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3509967/pdf/f-68-01472.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31081143","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

Crystallization of the DdrB-DNA complex from Deinococcus radiodurans. 放射球菌 DdrB-DNA 复合物的结晶。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-12-01 Epub Date: 2012-11-14 DOI: 10.1107/S1744309112044041

Seiji Sugiman-Marangos, Murray Junop

引用次数: 0

A preliminary X-ray study of transketolase from Burkholderia pseudomallei. 假马勒伯克霍尔德氏菌转酮醇酶的 X 射线初步研究。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-12-01 Epub Date: 2012-11-28 DOI: 10.1107/S1744309112044375

Mi Sun Kim, Areum Lim, Seung Won Yang, Daeun Lee, Jimin Park, Dong Hae Shin

引用次数: 0

Crystallization and first data collection of the putative transfer protein TraN from the Gram-positive conjugative plasmid pIP501. 革兰氏阳性结合质粒pIP501推定转移蛋白TraN的结晶和首次数据收集。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-11-01 Epub Date: 2012-10-30 DOI: 10.1107/S174430911204184X

Nikolaus Goessweiner-Mohr, Christian Fercher, Mohammad Yaser Abajy, Elisabeth Grohmann, Walter Keller

引用次数: 5

Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of aspartyl aminopeptidase from the apeB gene of Pseudomonas aeruginosa. Retraction. 铜绿假单胞菌apeB基因天冬氨酸氨基肽酶的克隆、表达、结晶及初步x射线晶体学分析。收缩。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-11-01 Epub Date: 2012-10-31 DOI: 10.1107/S1744309112039875

引用次数: 0

Solution structure of the cold-shock-like protein from Rickettsia rickettsii. 立克次体冷冲击样蛋白的溶液结构。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-11-01 Epub Date: 2012-10-26 DOI: 10.1107/S174430911203881X

Kyle P Gerarden, Andrew M Fuchs, Jonathan M Koch, Melissa M Mueller, David R Graupner, Justin T O'Rorke, Caleb D Frost, Heather A Heinen, Emily R Lackner, Scott J Schoeller, Paul G House, Francis C Peterson, Christopher T Veldkamp

{"title":"Solution structure of the cold-shock-like protein from Rickettsia rickettsii.","authors":"Kyle P Gerarden, Andrew M Fuchs, Jonathan M Koch, Melissa M Mueller, David R Graupner, Justin T O'Rorke, Caleb D Frost, Heather A Heinen, Emily R Lackner, Scott J Schoeller, Paul G House, Francis C Peterson, Christopher T Veldkamp","doi":"10.1107/S174430911203881X","DOIUrl":"https://doi.org/10.1107/S174430911203881X","url":null,"abstract":"Rocky Mountain spotted fever is caused by Rickettsia rickettsii infection. R. rickettsii can be transmitted to mammals, including humans, through the bite of an infected hard-bodied tick of the family Ixodidae. Since the R. rickettsii genome contains only one cold-shock-like protein and given the essential nature of cold-shock proteins in other bacteria, the structure of the cold-shock-like protein from R. rickettsii was investigated. With the exception of a short α-helix found between β-strands 3 and 4, the solution structure of the R. rickettsii cold-shock-like protein has the typical Greek-key five-stranded β-barrel structure found in most cold-shock domains. Additionally, the R. rickettsii cold-shock-like protein, with a ΔG of unfolding of 18.4 kJ mol(-1), has a similar stability when compared with other bacterial cold-shock proteins.","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":"68 Pt 11","pages":"1284-8"},"PeriodicalIF":0.9,"publicationDate":"2012-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S174430911203881X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31042788","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: 4

Crystallization and preliminary X-ray crystallographic analysis of an ice-binding protein (FfIBP) from Flavobacterium frigoris PS1. Addendum 冷冻黄杆菌PS1中冰结合蛋白(FfIBP)的结晶及初步x射线晶体学分析。齿顶高

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-10-31 DOI: 10.1107/S1744309112036482

H. Do, J. Lee, S. G. Lee, H. Kim

引用次数: 15

Recombinant portal protein from Staphylococcus epidermidis bacteriophage CNPH82 is a 13-subunit oligomer. 来自表皮葡萄球菌噬菌体CNPH82的重组门蛋白是一个13个亚基的低聚物。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-10-01 Epub Date: 2012-09-29 DOI: 10.1107/S1744309112037645

Weisha Luan, Jochen Fesseler, Maria Chechik, Carina R Buttner, Alfred A Antson, Callum Smits

引用次数: 3