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Science 10 May 2002:
Vol. 296. no. 5570, pp. 1091 - 1098
DOI: 10.1126/science.1071142
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Research Articles

The E. coli BtuCD Structure: A Framework for ABC Transporter Architecture and Mechanism

Kaspar P. Locher,* Allen T. Lee, Douglas C. Rees*

The ABC transporters are ubiquitous membrane proteins that couple adenosine triphosphate (ATP) hydrolysis to the translocation of diverse substrates across cell membranes. Clinically relevant examples are associated with cystic fibrosis and with multidrug resistance of pathogenic bacteria and cancer cells. Here, we report the crystal structure at 3.2 angstrom resolution of the Escherichia coli BtuCD protein, an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and appears to represent a conserved motif among the ABC transporters.

Howard Hughes Medical Institute and Division of Chemistry and Chemical Engineering, Mail Code 147-75CH, California Institute of Technology, Pasadena, CA 91125, USA.
*   To whom correspondence should be addressed. E-mail: locher{at}caltech.edu, dcrees{at}caltech.edu

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Functional Roles of Nonconserved Structural Segments in CFTR's NH2-terminal Nucleotide Binding Domain.
L. Csanady, K. W. Chan, A. C. Nairn, and D. C. Gadsby (2004)
J. Gen. Physiol. 125, 43-55
   Abstract »    Full Text »    PDF »
Identification and Characterization of Functionally Important Elements in the Multidrug Resistance Protein 1 COOH-terminal Region.
C. J. Westlake, L. Payen, M. Gao, S. P. C. Cole, and R. G. Deeley (2004)
J. Biol. Chem. 279, 53571-53583
   Abstract »    Full Text »    PDF »
The mechanism of ammonia transport based on the crystal structure of AmtB of Escherichia coli.
L. Zheng, D. Kostrewa, S. Berneche, F. K. Winkler, and X.-D. Li (2004)
PNAS 101, 17090-17095
   Abstract »    Full Text »    PDF »
Toward Linking Structure With Function in ATP-Sensitive K+ Channels.
J. Bryan, W. H. Vila-Carriles, G. Zhao, A. P. Babenko, and L. Aguilar-Bryan (2004)
Diabetes 53, S104-S112
   Abstract »    Full Text »    PDF »
ATP-binding Cassette Transporter A1 Contains a Novel C-terminal VFVNFA Motif That Is Required for Its Cholesterol Efflux and ApoA-I Binding Activities.
M. L. Fitzgerald, K.-i. Okuhira, G. F. Short III, J. J. Manning, S. A. Bell, and M. W. Freeman (2004)
J. Biol. Chem. 279, 48477-48485
   Abstract »    Full Text »    PDF »
Properties of P-glycoprotein with Mutations in the "Catalytic Carboxylate" Glutamate Residues.
G. Tombline, L. A. Bartholomew, G. A. Tyndall, K. Gimi, I. L. Urbatsch, and A. E. Senior (2004)
J. Biol. Chem. 279, 46518-46526
   Abstract »    Full Text »    PDF »
A Three-Dimensional Model for the Substrate Binding Domain of the Multidrug ATP Binding Cassette Transporter LmrA.
G. F. Ecker, K. Pleban, S. Kopp, E. Csaszar, G. J. Poelarends, M. Putman, D. Kaiser, W. N. Konings, and P. Chiba (2004)
Mol. Pharmacol. 66, 1169-1179
   Abstract »    Full Text »    PDF »
The Evolutionary Repertoires of the Eukaryotic-Type ABC Transporters in Terms of the Phylogeny of ATP-binding Domains in Eukaryotes and Prokaryotes.
Y. Igarashi, K. F. Aoki, H. Mamitsuka, K.-i. Kuma, and M. Kanehisa (2004)
Mol. Biol. Evol. 21, 2149-2160
   Abstract »    Full Text »    PDF »
Conformational Transitions Induced by the Binding of MgATP to the Vitamin B12 ATP-binding Cassette (ABC) Transporter BtuCD.
E. O. Oloo and D. P. Tieleman (2004)
J. Biol. Chem. 279, 45013-45019
   Abstract »    Full Text »    PDF »


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