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POTRA domain structure and function by NMR spectroscopy

POTRA 结构域结构和功能的 NMR 光谱分析

基本信息

批准号：
BB/F000472/1
负责人：
Michael Overduin
金额：
$ 47.84万
依托单位：
University of Birmingham
依托单位国家：
英国
项目类别：
Research Grant
财政年份：
2007
资助国家：
英国
起止时间：
2007 至无数据
项目状态：
已结题

来源：
https://gtr.ukri.org/projects?ref=BB%2FF000472%2F1
关键词：
POTRA domain structure function NMR

项目摘要

In this research project, the three dimensional structures and biochemical functions of proteins found in the outer membrane of Gram-negative bacteria will be analyzed by spectroscopic methods. The proteins are known as autotransporters. They are responsible for the secretion of materials out of the bacterial cell and into the outer membrane and surrounding environment. Here we focus on a component of these proteins called the POTRA domain which is thought to be responsible for recruiting bacterial proteins for secretion. Gram negative bacteria are characterized by an outer membrane that surrounds a polymeric network known as peptidoglycan. The main function of the outer membrane is to form a semi-permeable layer around the peptidoglycan to protect the bacterial cell. Proteins are inserted into the outer membrane in order to control its permeability. The analysis of many bacterial genomes has revealed that POTRA domain-containing autotransporters are universally found in outer membranes of Gram negative bacteria, and are essential for their survival. In fact, this system is the most widely used protein secretion system within all Gram-negative bacteria. The POTRA domain-containing autotransporters are needed to form bacterial outer membranes and to insert proteins correctly. Some of the proteins inserted into the outer membrane of pathogenic bacteria are important antigens that act as targets of protective immune responses. Understanding how the POTRA domain recognizes and assembles these proteins is important for targeting pathogenic bacteria and for manipulating the immune response during a bacterial infection. The outer membranes of different types of Gram-negative bacteria contain a variety of lipids in addition to proteins. The outer leaflet is composed of lipopolysaccharides, glycolipids and phospholipids which differ between bacterial species. The type of lipid in the outer membrane is essential for the assembly of proteins into the membrane, and also have important roles in immune response. Consequently, we will also investigate the role of the lipids and membrane on POTRA domains, which exist next to the membrane and help to usher proteins into and through the membrane, in order to better understand how POTRA domains are oriented and active at the membrane surface.

在该研究项目中，将通过光谱方法分析革兰氏阴性细菌外膜中蛋白质的三维结构和生化功能。这些蛋白质被称为自转运蛋白。它们负责将物质从细菌细胞分泌到外膜和周围环境中。在这里，我们重点关注这些蛋白质的一个组成部分，称为 POTRA 结构域，它被认为负责招募细菌蛋白质进行分泌。革兰氏阴性细菌的特征是外膜包围着称为肽聚糖的聚合物网络。外膜的主要功能是在肽聚糖周围形成半透层，以保护细菌细胞。将蛋白质插入外膜以控制其渗透性。对许多细菌基因组的分析表明，含有 POTRA 结构域的自转运蛋白普遍存在于革兰氏阴性细菌的外膜中，并且对其生存至关重要。事实上，该系统是所有革兰氏阴性细菌中使用最广泛的蛋白质分泌系统。需要含有 POTRA 结构域的自转运蛋白来形成细菌外膜并正确插入蛋白质。插入病原菌外膜的一些蛋白质是重要的抗原，可作为保护性免疫反应的目标。了解 POTRA 结构域如何识别和组装这些蛋白质对于靶向致病细菌和在细菌感染期间操纵免疫反应非常重要。不同类型的革兰氏阴性菌的外膜除蛋白质外还含有多种脂质。外层小叶由脂多糖、糖脂和磷脂组成，这些成分因细菌种类而异。外膜中的脂质类型对于蛋白质组装到膜中至关重要，并且在免疫反应中也具有重要作用。因此，我们还将研究脂质和膜对 POTRA 结构域的作用，POTRA 结构域存在于膜旁边，有助于引导蛋白质进入和穿过膜，以便更好地了解 POTRA 结构域如何在膜表面定向和活跃。

项目成果

期刊论文数量（10）

专著数量（0）

科研奖励数量（0）

会议论文数量（0）

专利数量（0）

Secondary structure and 1H, 13C and 15N resonance assignments of BamE, a component of the outer membrane protein assembly machinery in Escherichia coli

DOI：
10.1007/s12104-010-9236-7
发表时间：
2010-10-01
期刊：
BIOMOLECULAR NMR ASSIGNMENTS
影响因子：
0.9
作者：
Knowles, Timothy J.;Sridhar, Pooja;Henderson, Ian R.
通讯作者：
Henderson, Ian R.

Expression, Purification, and Screening of BamE, a Component of the BAM Complex, for Structural Characterization.

BamE（BAM 复合物的一个组成部分）的表达、纯化和筛选，用于结构表征。

DOI：
10.1007/978-1-4939-2871-2_19
发表时间：
2015
期刊：
Methods in molecular biology (Clifton, N.J.)
影响因子：
0
作者：
Jeeves M
通讯作者：
Jeeves M

Mutational and topological analysis of the Escherichia coli BamA protein.

DOI：
10.1371/journal.pone.0084512
发表时间：
2013
期刊：
PloS one
影响因子：
3.7
作者：
Browning DF;Matthews SA;Rossiter AE;Sevastsyanovich YR;Jeeves M;Mason JL;Wells TJ;Wardius CA;Knowles TJ;Cunningham AF;Bavro VN;Overduin M;Henderson IR
通讯作者：
Henderson IR

Secondary structure and 1H, 13C and 15N resonance assignments of the Escherichia coli YaeT POTRA domain.

大肠杆菌 YaeT POTRA 结构域的二级结构以及 1H、13C 和 15N 共振分配。