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Snapshots of the maltose transporter during ATP hydrolysis.

Oldham ML, Chen J
Proc Natl Acad Sci U S A 108 15152-6 (2011)
Related entries: 3puv, 3pux, 3rlf

Cited: 124 times
EuropePMC logo PMID: 21825153

Abstract

ATP-binding cassette transporters are powered by ATP, but the mechanism by which these transporters hydrolyze ATP is unclear. In this study, four crystal structures of the full-length wild-type maltose transporter, stabilized by adenosine 5'-(β,γ-imido)triphosphate or ADP in conjunction with phosphate analogs BeF(3)(-), VO(4)(3-), or AIF(4)(-), were determined to 2.2- to 2.4-Å resolution. These structures led to the assignment of two enzymatic states during ATP hydrolysis and demonstrate specific functional roles of highly conserved residues in the nucleotide-binding domain, suggesting that ATP-binding cassette transporters catalyze ATP hydrolysis via a general base mechanism.

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Articles - 3puw mentioned but not cited (9)

  1. Snapshots of the maltose transporter during ATP hydrolysis. Oldham ML, Chen J. Proc. Natl. Acad. Sci. U.S.A. 108 15152-15156 (2011)
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