8QP5

Release Complex: BAM bound EspP (SurA released)

8QP5 の概要

• エントリーDOI: 10.2210/pdb8qp5/pdb
• 関連するPDBエントリー: 8PZ1 8PZ2 8PZU 8PZV 8Q0G
• EMDBエントリー: 18034 18035 18045 18046 18053 18543
• 分子名称: Outer membrane protein assembly factor BamA, Outer membrane protein assembly factor BamB, Outer membrane protein assembly factor BamC, ... (6 entities in total)
• 機能のキーワード: outer membrane, complex, chaperone, protein folding, membrane protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 289423.38

構造登録者

Fenn, K.L.,Ranson, N.A. (登録日: 2023-09-29, 公開日: 2024-09-25)

主引用文献

Fenn, K.L.,Horne, J.E.,Crossley, J.A.,Bohringer, N.,Horne, R.J.,Schaberle, T.F.,Calabrese, A.N.,Radford, S.E.,Ranson, N.A.
Outer membrane protein assembly mediated by BAM-SurA complexes.
Nat Commun, 15:7612-7612, 2024

PubMed Abstract: The outer membrane is a formidable barrier that protects Gram-negative bacteria against environmental threats. Its integrity requires the correct folding and insertion of outer membrane proteins (OMPs) by the membrane-embedded β-barrel assembly machinery (BAM). Unfolded OMPs are delivered to BAM by the periplasmic chaperone SurA, but how SurA and BAM work together to ensure successful OMP delivery and folding remains unclear. Here, guided by AlphaFold2 models, we use disulphide bond engineering in an attempt to trap SurA in the act of OMP delivery to BAM, and solve cryoEM structures of a series of complexes. The results suggest that SurA binds BAM at its soluble POTRA-1 domain, which may trigger conformational changes in both BAM and SurA that enable transfer of the unfolded OMP to the BAM lateral gate for insertion into the outer membrane. Mutations that disrupt the interaction between BAM and SurA result in outer membrane assembly defects, supporting the key role of SurA in outer membrane biogenesis.

PubMed: 39218969
DOI: 10.1038/s41467-024-51358-x

実験手法

ELECTRON MICROSCOPY (4.4 Å)