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首页> 外文期刊>Journal of Molecular Biology >The Crystal Structure of Helicobacter Cysteine-rich Protein C at 2.0A Resolution: Similar Peptide-binding Sites in TPR and SEL1-like Repeat Proteins.
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The Crystal Structure of Helicobacter Cysteine-rich Protein C at 2.0A Resolution: Similar Peptide-binding Sites in TPR and SEL1-like Repeat Proteins.

机译：在2.0A分辨率下，富含半胱氨酸的半胱氨酸蛋白C的晶体结构：TPR和SEL1样重复蛋白中相似的肽结合位点。

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Helicobacter pylori is a Gram-negative human pathogen that infects the gastric mucosa and causes an inflammatory process leading to gastritis, ulceration and cancer. Bacterial cell-surface and secreted proteins often play an important role in pathogen-host interactions and are thought to be selective mediators for the pathology of the infection. The Helicobacter cysteine-rich proteins (Hcp) represent a large family of secreted proteins that seem to be specific for microorganisms from the -subfamily of proteobacteria. Although significantly elevated levels of anti-Hcp antibodies were observed in many patients infected with H.pylori, details on the biological functions of Hcp proteins are sparse. Hcps belong to a large family of Sel1-like multi-repeat proteins. The crystal structure of HcpC was refined at 2.0A resolution and revealed a super-helical topology composed of seven disulfide bridged alpha/alpha-repeats, an N-terminal capping helix and an extended C-terminal coil consisting of alternating hydrophobic and hydrophilic residues. In the crystal packing, the C-terminal coil interacts with the concave surface of a symmetry-related HcpC super-helix. A hydrophobic pocket and a cluster of negatively charged residues recognize the side-chains of Val290 and Lys287 from the C-terminal coil, respectively. The peptide nitrogen atom of His291 forms a short hydrogen bond with the side-chain of Asn66. The interactions seen in this crystal contact are strikingly similar to the peptide-binding modes of the Hsp70/Hsp90 organizing protein and the PEX5 receptor. The conservation of the peptide-binding mode suggests that HcpC might recognize its binding partner in a similar way.
机译：幽门螺杆菌是一种革兰氏阴性人类病原体，可感染胃粘膜并引起导致胃炎，溃疡和癌症的炎症过程。细菌细胞表面和分泌的蛋白质通常在病原体与宿主的相互作用中起重要作用，并被认为是感染病理的选择性介体。富含半胱氨酸的幽门螺杆菌（Hcp）代表着一大类分泌的蛋白质，这些蛋白质似乎特异于蛋白杆菌亚家族的微生物。尽管在许多感染幽门螺杆菌的患者中观察到抗Hcp抗体的水平显着升高，但是有关Hcp蛋白生物学功能的细节很少。 Hcps属于Sel1样多重复蛋白的大家族。 HcpC的晶体结构以2.0A的分辨率精制，显示出超螺旋拓扑结构，该拓扑结构由七个二硫键桥接的alpha / alpha重复序列，一个N端帽螺旋和一个由交替的疏水和亲水残基组成的扩展C端线圈组成。在晶体堆积中，C端线圈与对称相关的HcpC超螺旋的凹面相互作用。疏水口袋和带负电荷的残基簇分别从C末端线圈识别Val290和Lys287的侧链。 His291的肽氮原子与Asn66的侧链形成一个短氢键。在这种晶体接触中看到的相互作用非常类似于Hsp70 / Hsp90组织蛋白和PEX5受体的肽结合模式。肽结合模式的保守性提示HcpC可能以类似方式识别其结合伴侣。

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