7KO9

Crystal structure of antigen 43 from uropathogenic Escherichia coli UTI89

7KO9 の概要

• エントリーDOI: 10.2210/pdb7ko9/pdb
• 分子名称: AidA-I family adhesin, GLYCEROL, ISOPROPYL ALCOHOL, ... (6 entities in total)
• 機能のキーワード: autotransporters, biofilm, bacterial virulence, bacterial infection, microbial protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57306.61

構造登録者

Vo, J.L.,Hor, L.,Paxman, J.J.,Heras, B. (登録日: 2020-11-07, 公開日: 2022-03-09, 最終更新日: 2023-10-25)

主引用文献

Vo, J.L.,Ortiz, G.C.M.,Totsika, M.,Lo, A.W.,Hancock, S.J.,Whitten, A.E.,Hor, L.,Peters, K.M.,Ageorges, V.,Caccia, N.,Desvaux, M.,Schembri, M.A.,Paxman, J.J.,Heras, B.
Variation of Antigen 43 self-association modulates bacterial compacting within aggregates and biofilms.
NPJ Biofilms Microbiomes, 8:20-20, 2022

PubMed Abstract: The formation of aggregates and biofilms enhances bacterial colonisation and infection progression by affording protection from antibiotics and host immune factors. Despite these advantages there is a trade-off, whereby bacterial dissemination is reduced. As such, biofilm development needs to be controlled to suit adaptation to different environments. Here we investigate members from one of largest groups of bacterial adhesins, the autotransporters, for their critical role in the assembly of bacterial aggregates and biofilms. We describe the structural and functional characterisation of autotransporter Ag43 variants from different Escherichia coli pathotypes. We show that specific interactions between amino acids on the contacting interfaces of adjacent Ag43 proteins drives a common mode of trans-association that leads to cell clumping. Furthermore, subtle variation of these interactions alters aggregation kinetics and the degree of compacting within cell clusters. Together, our structure-function investigation reveals an underlying molecular basis for variations in the density of bacterial communities.

PubMed: 35396507
DOI: 10.1038/s41522-022-00284-1

実験手法

X-RAY DIFFRACTION (2.43 Å)