The 1.2 ? resolution crystal structure of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera-toxin production

WaldenP.M.; HerasB.; ChenK.-E.HaliliM.A.RimmerK.SharmaP.ScanlonM.J.MartinJ.L.

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The 1.2 ? resolution crystal structure of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera-toxin production

机译：1.2吗?霍乱弧菌的DsbA disulfide-forming纤毛和霍乱毒素所需的蛋白质生产

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The enzyme TcpG is a periplasmic protein produced by the Gram-negative pathogen Vibrio cholerae. TcpG is essential for the production of ToxR-regulated proteins, including virulence-factor pilus proteins and cholera toxin, and is therefore a target for the development of a new class of anti-virulence drugs. Here, the 1.2 ? resolution crystal structure of TcpG is reported using a cryocooled crystal. This structure is compared with a previous crystal structure determined at 2.1 ? resolution from data measured at room temperature. The new crystal structure is the first DsbA crystal structure to be solved at a sufficiently high resolution to allow the inclusion of refined H atoms in the model. The redox properties of TcpG are also reported, allowing comparison of its oxidoreductase activity with those of other DSB proteins. One of the defining features of the Escherichia coli DsbA enzyme is its destabilizing disulfide, and this is also present in TcpG. The data presented here provide new insights into the structure and redox properties of this enzyme, showing that the binding mode identified between E. coli DsbB and DsbA is likely to be conserved in TcpG and that the Β5-7 loop near the proposed DsbB binding site is flexible, and suggesting that the tense oxidized conformation of TcpG may be the consequence of a short contact at the active site that is induced by disulfide formation and is relieved by reduction.

机译：这种酶TcpG周质蛋白由革兰氏阴性病菌霍乱弧菌。TcpG生产至关重要ToxR-regulated蛋白质,包括virulence-factor菌毛蛋白和霍乱毒素,因此一个目标anti-virulence发展的一个新类药物。使用cryocooled TcpG结构报道晶体。以前的晶体结构决定在2.1吗?分辨率的数据测量的房间温度。第一个DsbA晶体结构需要解决的足够的高分辨率的允许精制的H原子模型中。氧化还原性质TcpG也报道,允许其氧化还原酶的比较活动与其他双边带蛋白质。大肠杆菌的定义特征二硫化DsbA酶是其不稳定,这也是在TcpG。这里提供新的见解和结构这种酶的氧化还原特性,显示绑定模式识别和大肠杆菌DsbB之间在TcpG DsbA可能是守恒的,Β5 - 7循环提出DsbB结合位点附近是灵活的,这表明紧张吗氧化TcpG可能构象活性位点的短暂接触的结果二硫形成和诱导的通过减少缓解。

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《Acta crystallographica.Section D. Biological crystallography》 |2012年第10期|1290-1302|共13页
作者
WaldenP.M.; HerasB.; ChenK.-E.HaliliM.A.RimmerK.SharmaP.ScanlonM.J.MartinJ.L.;
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Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal;

Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, University of;

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正文语种英语
中图分类化学;
关键词
Protein-Protein Interaction; Oxidoreductases; VirulenceRedox propertiescrystal structureBiological ToxinsPilusVibrio choleraePeriplasmic Proteins;

机译：蛋白质交互;氧化还原酶;VirulenceRedoxpropertiescrystal structureBiologicalToxinsPilusVibrio choleraePeriplasmic蛋白质;

The 1.2 ? resolution crystal structure of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera-toxin production

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