5AYW
Structure of a membrane complex
Summary for 5AYW
Entry DOI | 10.2210/pdb5ayw/pdb |
Descriptor | Outer membrane protein assembly factor BamA, Outer membrane protein assembly factor BamB, Outer membrane protein assembly factor BamC, ... (5 entities in total) |
Functional Keywords | membrane protein, complex, membrane biogenesis |
Biological source | Escherichia coli (strain K12) More |
Cellular location | Cell outer membrane : P0A940 Cell outer membrane ; Lipid-anchor : P77774 P0A903 P0AC02 P0A937 |
Total number of polymer chains | 5 |
Total formula weight | 172548.46 |
Authors | |
Primary citation | Han, L.,Zheng, J.,Wang, Y.,Yang, X.,Liu, Y.,Sun, C.,Cao, B.,Zhou, H.,Ni, D.,Lou, J.,Zhao, Y.,Huang, Y. Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins Nat.Struct.Mol.Biol., 23:192-196, 2016 Cited by PubMed Abstract: In Gram-negative bacteria, the assembly of β-barrel outer-membrane proteins (OMPs) requires the β-barrel-assembly machinery (BAM) complex. We determined the crystal structure of the 200-kDa BAM complex from Escherichia coli at 3.55-Å resolution. The structure revealed that the BAM complex assembles into a hat-like shape, in which the BamA β-barrel domain forms the hat's crown embedded in the outer membrane, and its five polypeptide transport-associated (POTRA) domains interact with the four lipoproteins BamB, BamC, BamD and BamE, thus forming the hat's brim in the periplasm. The assembly of the BAM complex creates a ring-like apparatus beneath the BamA β-barrel in the periplasm and a potential substrate-exit pore located at the outer membrane-periplasm interface. The complex structure suggests that the chaperone-bound OMP substrates may feed into the chamber of the ring-like apparatus and insert into the outer membrane via the potential substrate-exit pore in an energy-independent manner. PubMed: 26900875DOI: 10.1038/nsmb.3181 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.555 Å) |
Structure validation
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