9CX4

Acinetobacter baumannii BamA POTRAs 1-4, space group P1

9CX4 の概要

• エントリーDOI: 10.2210/pdb9cx4/pdb
• 分子名称: Outer membrane protein assembly factor BamA (2 entities in total)
• 機能のキーワード: membrane protein, transport, protein transport
• 由来する生物種: Acinetobacter baumannii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74759.12

構造登録者

Overly Cottom, C.,Noinaj, N. (登録日: 2024-07-30, 公開日: 2024-10-16, 最終更新日: 2024-11-27)

主引用文献

Cottom, C.O.,Stephenson, R.,Ricci, D.,Yang, L.,Gumbart, J.C.,Noinaj, N.
Structural characterization of the POTRA domains from A. baumannii reveals new conformations in BamA.
Structure, 32:2038-, 2024

PubMed Abstract: Recent studies have demonstrated BamA, the central component of the β-barrel assembly machinery (BAM), as an important therapeutic target to combat infections caused by Acinetobacter baumannii and other Gram-negative pathogens. Homology modeling indicates BamA in A. baumannii consists of five polypeptide transport-associated (POTRA) domains and a β-barrel membrane domain. We characterized the POTRA domains of BamA from A. baumannii in solution using size-exclusion chromatography small angle X-ray scattering (SEC-SAXS) analysis and determined crystal structures in two conformational states that are drastically different than those previously observed in BamA from other bacteria, indicating that the POTRA domains are even more conformationally dynamic than has been observed previously. Molecular dynamics simulations of the POTRA domains from A. baumannii and Escherichia coli allowed us to identify key structural features that contribute to the observed novel states. Together, these studies expand on our current understanding of the conformational plasticity within BamA across differing bacterial species.

PubMed: 39293443
DOI: 10.1016/j.str.2024.08.013

実験手法

X-RAY DIFFRACTION (2.78 Å)