Crystal structure of a catalytic intermediate of the maltose transporter

Michael L. Oldham, Dheeraj Khare, Florante A. Quiocho, Amy L. Davidson and Jue Chen ()
Additional contact information
Michael L. Oldham: Department of Biological Sciences,
Dheeraj Khare: Department of Biological Sciences,
Florante A. Quiocho: Baylor College of Medicine, Houston, Texas 77030, USA
Amy L. Davidson: Purdue University, West Lafayette, Indiana 47907, USA
Jue Chen: Department of Biological Sciences,

Nature, 2007, vol. 450, issue 7169, 515-521

Abstract: Abstract The maltose uptake system of Escherichia coli is a well-characterized member of the ATP-binding cassette transporter superfamily. Here we present the 2.8-Å crystal structure of the intact maltose transporter in complex with the maltose-binding protein, maltose and ATP. This structure, stabilized by a mutation that prevents ATP hydrolysis, captures the ATP-binding cassette dimer in a closed, ATP-bound conformation. Maltose is occluded within a solvent-filled cavity at the interface of the two transmembrane subunits, about halfway into the lipid bilayer. The binding protein docks onto the entrance of the cavity in an open conformation and serves as a cap to ensure unidirectional translocation of the sugar molecule. These results provide direct evidence for a concerted mechanism of transport in which solute is transferred from the binding protein to the transmembrane subunits when the cassette dimer closes to hydrolyse ATP.

Date: 2007
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/nature06264 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:450:y:2007:i:7169:d:10.1038_nature06264

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature06264

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().