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Nat Struct Mol Biol. 2012 Apr 8;19(5):538-46, S1. doi: 10.1038/nsmb.2278.

ATP binding controls distinct structural transitions of Escherichia coli DNA gyrase in complex with DNA.

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  • 1Department of Applied Physics, Stanford University, Stanford, California, USA.

Abstract

DNA gyrase is a molecular motor that harnesses the free energy of ATP hydrolysis to introduce negative supercoils into DNA. A critical step in this reaction is the formation of a chiral DNA wrap. Here we observe gyrase structural dynamics using a single-molecule assay in which gyrase drives the processive, stepwise rotation of a nanosphere attached to the side of a stretched DNA molecule. Analysis of rotational pauses and measurements of DNA contraction reveal multiple ATP-modulated structural transitions. DNA wrapping is coordinated with the ATPase cycle and proceeds by way of an unanticipated structural intermediate that dominates the kinetics of supercoiling. Our findings reveal a conformational landscape of loosely coupled transitions funneling the motor toward productive energy transduction, a feature that may be common to the reaction cycles of other DNA and protein remodeling machines.

PMID:
22484318
[PubMed - indexed for MEDLINE]
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