Structural highlights
FunctionA0A6F8TEF0_ACIBA Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.[HAMAP-Rule:MF_01430] Publication Abstract from PubMedRecent studies have demonstrated BamA, the central component of the beta-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 beta-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. Structural characterization of the POTRA domains from A. baumannii reveals new conformations in BamA.,Cottom CO, Stephenson R, Ricci D, Yang L, Gumbart JC, Noinaj N Structure. 2024 Sep 10:S0969-2126(24)00330-7. doi: 10.1016/j.str.2024.08.013. PMID:39293443[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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