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-Structure paper
タイトル | Outer membrane protein assembly mediated by BAM-SurA complexes. |
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ジャーナル・号・ページ | Nat Commun, Vol. 15, Issue 1, Page 7612, Year 2024 |
掲載日 | 2024年9月1日 |
著者 | Katherine L Fenn / Jim E Horne / Joel A Crossley / Nils Böhringer / Romany J Horne / Till F Schäberle / Antonio N Calabrese / Sheena E Radford / Neil A Ranson / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:39218969 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.9 - 5.3 Å |
構造データ | EMDB-18034, PDB-8pz1: EMDB-18035, PDB-8pz2: EMDB-18045, PDB-8pzu: EMDB-18046, PDB-8pzv: EMDB-18053, PDB-8q0g: EMDB-18543, PDB-8qp5: EMDB-18562, PDB-8qpu: EMDB-18563, PDB-8qpv: EMDB-18564, PDB-8qpw: |
化合物 | ChemComp-MG: ChemComp-HOH: |
由来 |
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キーワード | MEMBRANE PROTEIN / Outer Membrane / Complex / Chaperone / Protein Folding / Inhibitor |