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

Pinkett, H. W. and Lee, A. T. and Lum, P. and Locher, K. P. and Rees, D. C. (2007) An Inward-Facing Conformation of a Putative Metal-Chelate–Type ABC Transporter. Science, 315 (5810). pp. 373-377. ISSN 0036-8075. doi:10.1126/science.1133488. https://resolver.caltech.edu/CaltechAUTHORS:20141112-082347898

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Abstract

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.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1126/science.1133488DOIArticle
http://www.sciencemag.org/content/315/5810/373PublisherArticle
http://www.sciencemag.org/content/315/5810/373/suppl/DC1PublisherSupporting Online Material
ORCID:
AuthorORCID
Rees, D. C.0000-0003-4073-1185
Additional Information:© 2007 American Association for the Advancement of Science. Received 4 August 2006; accepted 30 November 2006 Published online 7 December 2006. We thank L. Thomas and J. Kaiser for their contributions to the structure determination, N. Kadaba and J. B. Howard for discussions, and the staff of the Stanford Synchrotron Radiation Laboratory (SSRL) for their assistance during crystal screening and data collection. This work was supported in part by NIH grant GM45162. We acknowledge support for fellowships from the James Irvine Foundation (H.W.P.) and NIH (P.L.), the Vallee Foundation (D.C.R.), the Parsons Foundation for computational resources, and the Gordon and Betty Moore Foundation for support of the Molecular Observatory at Caltech. SSRL is supported by DOE and NIH. Coordinates have been deposited in the Protein Data Bank (PDB) [www.rcsb.org/pdb; (31)] as entry 2NQ2 for release upon publication.
Funders:
Funding AgencyGrant Number
NIHGM45162
James Irvine FoundationUNSPECIFIED
Vallee FoundationUNSPECIFIED
Parsons FoundationUNSPECIFIED
Gordon and Betty Moore FoundationUNSPECIFIED
Department of Energy (DOE)UNSPECIFIED
Issue or Number:5810
DOI:10.1126/science.1133488
Record Number:CaltechAUTHORS:20141112-082347898
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20141112-082347898
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:51627
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:12 Nov 2014 21:57
Last Modified:10 Nov 2021 19:13

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