三聚体自体转运体黏附素与肽聚糖结合的质周蛋白复合物的形成

IF 6.2 Q1 Immunology and Microbiology
Shogo Yoshimoto , Jun Sasahara , Atsuo Suzuki , Junichi Kanie , Kotaro Koiwai , Andrei N. Lupas , Katsutoshi Hori
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引用次数: 0

摘要

三聚体autotransporter adhesion (TAAs)是一种广泛分布于革兰氏阴性菌的外膜蛋白,主要参与生物和非生物表面的粘附、细胞凝集和生物膜的形成。TAAs由分泌到细胞表面的乘客结构域和跨膜结构域组成,后者在OM中形成一个孔来分泌和固定乘客结构域。由于TAAs在分泌过程中与伴侣蛋白或专用辅助蛋白之间的相互作用是短暂的,因此认为TAAs在分泌后不与其他蛋白形成复合物而驻留在OM上。在这项研究中,我们旨在阐明不动杆菌TAA (AtaA)与肽聚糖(PG)结合的质周蛋白TpgA之间的相互作用。利用重组蛋白进行下拉分析,确定了相互作用结构域。2.6 Å分辨率的x射线晶体学显示了由TpgA的n端结构域和AtaA的跨膜结构域组成的A3B3杂六聚络合物结构。TpgA-N由两个短的α螺旋和三个反平行的β链组成,产生类似于BamE的ααββ拓扑结构。然而,在TpgA-N中,BamA和BamD的BamE接口对应的区域是不同的。全原子分子动力学模拟和突变分析表明,静电和疏水相互作用都有助于稳定的络合物形成。生物信息学分析表明,TAA-TpgA复合物存在于广泛的物种中。这些发现将有助于更好地理解TAAs和细胞包膜。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Insights into the complex formation of a trimeric autotransporter adhesin with a peptidoglycan-binding periplasmic protein
Trimeric autotransporter adhesins (TAAs) are outer membrane (OM) proteins that are widely distributed in gram-negative bacteria and are involved primarily in adhesion to biotic and abiotic surfaces, cell agglutination, and biofilm formation. TAAs consist of a passenger domain, which is secreted onto the cell surface, and a transmembrane domain, which forms a pore in the OM to secrete and anchor the passenger domain. Because the interactions between TAAs and chaperones or dedicated auxiliary proteins during secretion are short-lived, TAAs are thought to reside on the OM without forming complexes with other proteins after secretion. In this study, we aimed to clarify the interactions between an Acinetobacter TAA, AtaA, and a peptidoglycan (PG)-binding periplasmic protein, TpgA. Pull-down assays using recombinant proteins identified the interacting domains. X-ray crystallography at 2.6 Å resolution revealed an A3B3 heterohexameric complex structure composed of the N-terminal domain of TpgA and the transmembrane domain of AtaA. TpgA-N consists of two short α helices and three antiparallel β strands, yielding an ααβββ topology similar to BamE. However, the regions corresponding to BamE interfaces with BamA and BamD differ in TpgA-N. All-atom molecular dynamics simulations and mutational assays revealed that both electrostatic and hydrophobic interactions contribute to stable complex formation. Bioinformatic analyses indicate that the TAA-TpgA complex occurs in a wide range of species. These findings will contribute to a better understanding of TAAs and the cell envelope.
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来源期刊
Cell Surface
Cell Surface Immunology and Microbiology-Applied Microbiology and Biotechnology
CiteScore
6.10
自引率
0.00%
发文量
18
审稿时长
49 days
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