Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 23, Issue 3, Pages 192-196Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3181
Keywords
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Funding
- Ministry of Science and Technology [2012CB917302, 2013CB910603]
- Strategic Priority Research Program of the Chinese Academy of Sciences [XDB080202]
- National Natural Science Foundation of China [31170698, 31470743]
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In Gram-negative bacteria, the assembly of beta-barrel outer-membrane proteins (OMPs) requires the beta-barrel-assembly machinery (BAM) complex. We determined the crystal structure of the 200-kDa BAM complex from Escherichia coli at 3.55-angstrom resolution. The structure revealed that the BAM complex assembles into a hat-like shape, in which the BamA beta-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 beta-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.
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