Crystal structure of bacterial multidrug efflux transporter AcrB View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-10

AUTHORS

Satoshi Murakami, Ryosuke Nakashima, Eiki Yamashita, Akihito Yamaguchi

ABSTRACT

AcrB is a major multidrug exporter in Escherichia coli. It cooperates with a membrane fusion protein, AcrA, and an outer membrane channel, TolC. We have determined the crystal structure of AcrB at 3.5 A resolution. Three AcrB protomers are organized as a homotrimer in the shape of a jellyfish. Each protomer is composed of a transmembrane region 50 A thick and a 70 A protruding headpiece. The top of the headpiece opens like a funnel, where TolC might directly dock into AcrB. A pore formed by three alpha-helices connects the funnel with a central cavity located at the bottom of the headpiece. The cavity has three vestibules at the side of the headpiece which lead into the periplasm. In the transmembrane region, each protomer has twelve transmembrane alpha-helices. The structure implies that substrates translocated from the cell interior through the transmembrane region and from the periplasm through the vestibules are collected in the central cavity and then actively transported through the pore into the TolC tunnel. More... »

PAGES

587

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nature01050

DOI

http://dx.doi.org/10.1038/nature01050

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1037353512

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/12374972


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