Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism

Science

Volumn 313, Issue 5791, 2006, Pages 1295-1298

  Seeger, Markus A ^a,c   Schiefner, André ^b,d   Eicher, Thomas ^a   Verrey, François ^a   Diederichs, Kay ^b   Pos, Klaas M ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

^b UNIVERSITY OF KONSTANZ   (Germany)

^c ETH ZURICH   (Switzerland)

^d SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTICS; CRYSTALLOGRAPHY; DETERGENTS; DRUG PRODUCTS; MONOMERS; ORGANIC SOLVENTS;

ANGSTROM RESOLUTION; DRUG TRANSPORT; PERISTALTIC MODE; PERISTALTIC PUMP MECHANISM;

ESCHERICHIA COLI;

ABC TRANSPORTER; ACRA PROTEIN; ACRB PROTEIN; ADENOSINE TRIPHOSPHATE; ANTIBIOTIC AGENT; BACTERIORHODOPSIN; MONOMER; OUTER MEMBRANE PROTEIN; PROTON; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; TOLC PROTEIN; UNCLASSIFIED DRUG;

ANTIBIOTICS; COLIFORM BACTERIUM; DRUG RESISTANCE; SOLVENT;

ANTIBIOTIC RESISTANCE; ARTICLE; BACTERIAL MEMBRANE; BACTERIAL OUTER MEMBRANE; BINDING AFFINITY; BINDING SITE; CRYSTAL STRUCTURE; DRUG TRANSPORT; ESCHERICHIA COLI; GRAM NEGATIVE BACTERIUM; MEMBRANE TRANSPORT; NONHUMAN; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY;

BIOLOGICAL TRANSPORT; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIFFUSION; DRUG RESISTANCE, MULTIPLE, BACTERIAL; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROGEN BONDING; HYDROPHOBICITY; MEMBRANE TRANSPORT PROTEINS; MODELS, MOLECULAR; MULTIDRUG RESISTANCE-ASSOCIATED PROTEINS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTONS;

ESCHERICHIA COLI;

EID: 33748310520     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1131542     Document Type: Article

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35. We thank the beamline staff at the Swiss Light Source (SLS) of the Paul Scherrer Institut in Villigen (Switzerland), and at the European Synchrotron Radiation Facility (ESRF) in Grenoble (France). This work was supported by a grant of the Transregio-Sonderforschungsbereich Zurich-Konstanz to K.D. We thank P. A. Karplus and W. Welte for critical reading and discussion. The atomic coordinates and structure factors of the C2 and P1 crystal forms have been deposited at the Protein Data Bank with accession numbers 2GIF and 2HRT, respectively. This work is dedicated to Peter Dimroth on the occasion of his 65th birthday.