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5AYW

Structure of a membrane complex

Summary for 5AYW
Entry DOI10.2210/pdb5ayw/pdb
DescriptorOuter membrane protein assembly factor BamA, Outer membrane protein assembly factor BamB, Outer membrane protein assembly factor BamC, ... (5 entities in total)
Functional Keywordsmembrane protein, complex, membrane biogenesis
Biological sourceEscherichia coli (strain K12)
More
Cellular locationCell outer membrane : P0A940
Cell outer membrane ; Lipid-anchor : P77774 P0A903 P0AC02 P0A937
Total number of polymer chains5
Total formula weight172548.46
Authors
Huang, Y.,Han, L.,Zheng, J. (deposition date: 2015-09-14, release date: 2016-02-24, Last modification date: 2024-03-20)
Primary citationHan, 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: 26900875
DOI: 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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