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Originally published in Science Express on 7 December 2006
Science 19 January 2007:
Vol. 315. no. 5810, pp. 373 - 377
DOI: 10.1126/science.1133488
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Reports

An Inward-Facing Conformation of a Putative Metal-Chelate-Type ABC Transporter

H. W. Pinkett,1 A. T. Lee,1 P. Lum,1* K. P. Locher,2 D. C. Rees1{dagger}

The crystal structure of a putative metal-chelate–type adenosine triphosphate (ATP)–binding cassette (ABC) transporter encoded by genes HI1470 and HI1471 of Haemophilus influenzae has been solved at 2.4 angstrom resolution. The permeation pathway exhibits an inward-facing conformation, in contrast to the outward-facing state previously observed for the homologous vitamin B12 importer BtuCD. Although the structures of both HI1470/1 and BtuCD have been solved in nucleotide-free states, the pairs of ABC subunits in these two structures differ by a translational shift in the plane of the membrane that coincides with a repositioning of the membrane-spanning subunits. The differences observed between these ABC transporters involve relatively modest rearrangements and may serve as structural models for inward- and outward-facing conformations relevant to the alternating access mechanism of substrate translocation.

1 Division of Chemistry and Chemical Engineering, Howard Hughes Medical Institute, MC 114-96, California Institute of Technology (Caltech), Pasadena, CA 91125, USA.
2 Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland.

* Present address: Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, USA.

{dagger} To whom correspondence should be addressed. E-mail: dcrees{at}caltech.edu

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