STRUCTURE AND FUNCTION OF OUTER MEMBRANE PROTEINS

外膜蛋白的结构和功能

• 批准号: 8169325
• 负责人: BERT VAN DEN BERG
• 金额: $ 0.35万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-04-01 至 2011-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8169325
• 关键词: Cell surface; Cleaved cell; Computer Retrieval of Information on Scientific Projects Database; Escherichia coli; Family; Funding; Gram-Negative Bacteria; Grant; Human; Institution; Length; Membrane; Membrane Proteins; Peptide Hydrolases; Physiological; Plasminogen; Plasminogen Activator; Pneumonic Plague; Proteins; Research; Research Personnel; Resolution; Resources; Role; Side; Source; Structure; Substrate Specificity; United States National Institutes of Health; Virulence; Virulence Factors; Yersinia pestis; base; extracellular; interest; member

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. A. Structure of the plasminogen activator Pla from Yersinia pestis. Pla is a member of the omptin family, a family of outer membrane proteases that is widespread in gram-negative bacteria. While the physiological role of most omptins (such as E. coli OmpT) is unclear, Y. pestis Pla has a proven, very important role in the virulence of both bubonic and pneumonic plague by cleaving (activation of) human plasminogen. We are investigatng the high-resolution crystal structure of Pla inorder to gain information into the catalytic mechanism of omptins and the structural basis for substrate specificity. B. Structure of a full-length autotransporter. The autotransporter secretion mechanism is the most common mechanism for the secretion of virulence factors across the outer membrane (OM) from pathogenic Gram-negative bacteria. In addition, autotransporters have attracted biotechnological and biomedical interest for protein display on bacterial cell surfaces. Despite their importance, the mechanism by which passenger domains of autotransporters pass the OM is still unclear. The classical view is that the ¿-barrel domain provides the conduit through which the unfolded passenger moves, with the energy provided by vectorial folding of the ¿-strand-rich passenger on the extracellular side of the OM.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 A.鼠疫耶尔森氏菌纤溶酶原激活物Pla的结构Pla是omptin家族的成员，omptin家族是广泛存在于革兰氏阴性细菌中的外膜蛋白酶家族。虽然大多数omptins（如E. coliOmpT），Y.鼠疫菌Pla通过切割（激活）人纤溶酶原，在腺鼠疫和肺鼠疫的毒力中具有已证实的非常重要的作用。 我们正在对Pla的高分辨率晶体结构进行分析，以获得有关omptins催化机制和底物特异性结构基础的信息。 B。全长自动运输机的结构。 自转运蛋白分泌机制是致病性革兰氏阴性菌跨外膜（OM）分泌毒力因子的最常见机制。此外，自体转运蛋白在细菌细胞表面的蛋白展示也吸引了生物技术和生物医学的兴趣。尽管它们的重要性，乘客域的autotorpers通过OM的机制仍不清楚。经典的观点是，桶结构域提供了未折叠乘客移动的管道，能量由OM细胞外侧富含链的乘客的矢量折叠提供。