9CX5

Acinetobacter baumannii BamA POTRAs 1-4, space group P3221

Summary for 9CX5

• Entry DOI: 10.2210/pdb9cx5/pdb
• Related: 9CX4
• Descriptor: Outer membrane protein assembly factor BamA (1 entity in total)
• Functional Keywords: membrane protein, transport, protein transport
• Biological source: Acinetobacter baumannii
• Total number of polymer chains: 2
• Total formula weight: 75213.64

Authors

Overly Cottom, C.,Noinaj, N. (deposition date: 2024-07-30, release date: 2024-10-30, Last modification date: 2024-11-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)