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-Structure paper
タイトル | Architecture and conformational dynamics of the BAM-SurA holo insertase complex. |
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ジャーナル・号・ページ | Sci Adv, Vol. 11, Issue 14, Page eads6094, Year 2025 |
掲載日 | 2025年4月4日 |
![]() | Philippe A Lehner / Morris Degen / Roman P Jakob / Seyed Majed Modaresi / Morgane Callon / Björn M Burmann / Timm Maier / Sebastian Hiller / ![]() |
PubMed 要旨 | The proper folding of outer membrane proteins in Gram-negative bacteria relies on their delivery to the β-barrel assembly machinery (BAM) complex. The mechanism by which survival protein A (SurA), ...The proper folding of outer membrane proteins in Gram-negative bacteria relies on their delivery to the β-barrel assembly machinery (BAM) complex. The mechanism by which survival protein A (SurA), the major periplasmic chaperone, facilitates this process is not well understood. We determine the structure of the holo insertase complex, where SurA binds BAM for substrate delivery. High-resolution cryo-electron microscopy structures of four different states and a three-dimensional variability analysis show that the holo insertase complex has a large motional spectrum. SurA bound to BAM can undergo a large swinging motion between two states. This motion is uncoupled from the conformational flexibility of the BamA barrel, which can open and close without affecting SurA binding. Notably, we observed conformational coupling of the SurA swing state and the carboxyl-terminal helix grip domain of BamC. Substrate delivery by SurA to BAM appears to follow a concerted motion that encodes a gated delivery pathway through the BAM accessory proteins to the membrane entry site. |
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手法 | EM (単粒子) |
解像度 | 2.73 - 3.62 Å |
構造データ | EMDB-52127, PDB-9hg6: EMDB-52128, PDB-9hg5: EMDB-52129, PDB-9hg7: EMDB-52130, PDB-9hg8: EMDB-52131, PDB-9hg9: EMDB-52132, PDB-9hga: |
化合物 | ![]() ChemComp-MG: |
由来 |
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![]() | MEMBRANE PROTEIN / insertase / outer membrane protein / chaperone / protein folding / protein complex / darobactin |