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Curr Opin Struct Biol. 2012 Apr;22(2):208-16. doi: 10.1016/j.sbi.2012.02.005. Epub 2012 Mar 16.

Structural insights into the Type II secretion nanomachine.

Author information

1
Department of Bacteriology, University of Wisconsin-Madison, Madison, WI, USA.

Abstract

The Type II secretion nanomachine transports folded proteins across the outer membrane of Gram-negative bacteria. Recent X-ray crystallography, electron microscopy, and molecular modeling studies provide structural insights into three functionally and spatially connected units of this nanomachine: the cytoplasmic and inner membrane energy-harvesting complex, the periplasmic helical pseudopilus, and the outer membrane secretin. Key advances include cryo-EM reconstruction of the secretin and demonstration that it interacts with both secreted substrates and a crucial transmembrane clamp protein, plus a biochemical and structural explanation of the role of low-abundance pseudopilins in initiating pseudopilus growth. Combining structures and protein interactions, we synthesize a 3D view of the complete complex consistent with a stepwise pathway in which secretin oligomerization defines sites of nanomachine biogenesis.

PMID:
22425326
PMCID:
PMC3341957
DOI:
10.1016/j.sbi.2012.02.005
[Indexed for MEDLINE]
Free PMC Article

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