6V4V

The crystal structure of BonA from Acinetobacter baumannii

6V4V の概要

• エントリーDOI: 10.2210/pdb6v4v/pdb
• 分子名称: BON domain protein, ZINC ION (3 entities in total)
• 機能のキーワード: periplasmic, lipoprotein, divisome protein, cell motility, outer-membrane stability, lipid binding protein
• 由来する生物種: Acinetobacter baumannii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20908.30

構造登録者

Grinter, R. (登録日: 2019-12-02, 公開日: 2021-06-02, 最終更新日: 2024-11-06)

主引用文献

Grinter, R.,Morris, F.C.,Dunstan, R.A.,Leung, P.M.,Kropp, A.,Belousoff, M.,Gunasinghe, S.D.,Scott, N.E.,Beckham, S.,Peleg, A.Y.,Greening, C.,Li, J.,Heinz, E.,Lithgow, T.
BonA from Acinetobacter baumannii Forms a Divisome-Localized Decamer That Supports Outer Envelope Function.
Mbio, :e0148021-e0148021, 2021

PubMed Abstract: Acinetobacter baumannii is a high-risk pathogen due to the rapid global spread of multidrug-resistant lineages. Its phylogenetic divergence from other ESKAPE pathogens means that determinants of its antimicrobial resistance can be difficult to extrapolate from other widely studied bacteria. A recent study showed that A. baumannii upregulates production of an outer membrane lipoprotein, which we designate BonA, in response to challenge with polymyxins. Here, we show that BonA has limited sequence similarity and distinct structural features compared to lipoproteins from other bacterial species. Analyses through X-ray crystallography, small-angle X-ray scattering, electron microscopy, and multiangle light scattering demonstrate that BonA has a dual BON (acterial smY and odulation) domain architecture and forms a decamer via an unusual oligomerization mechanism. This analysis also indicates this decamer is transient, suggesting dynamic oligomerization plays a role in BonA function. Antisera recognizing BonA shows it is an outer membrane protein localized to the divisome. Loss of BonA modulates the density of the outer membrane, consistent with a change in its structure or link to the peptidoglycan, and prevents motility in a clinical strain (ATCC 17978). Consistent with these findings, the dimensions of the BonA decamer are sufficient to permeate the peptidoglycan layer, with the potential to form a membrane-spanning complex during cell division. The pathogen Acinetobacter baumannii is considered an urgent threat to human health. A. baumannii is highly resistant to treatment with antibiotics, in part due to its protective cell envelope. This bacterium is only distantly related to other bacterial pathogens, so its cell envelope has distinct properties and contains components distinct from those of other bacteria that support its function. Here, we report the discovery of BonA, a protein that supports A. baumannii outer envelope function and is required for cell motility. We determine the atomic structure of BonA and show that it forms part of the cell division machinery and functions by forming a complex, features that mirror those of distantly related homologs from other bacteria. By improving our understanding of the A. baumannii cell envelope this work will assist in treating this pathogen.

PubMed: 34311571
DOI: 10.1128/mBio.01480-21

実験手法

X-RAY DIFFRACTION (1.65 Å)