Structure of the twin-arginine signal-binding protein DmsD from Escherichia coli

Abstract

The translocation of folded proteins via the twin-arginine translocation (Tat) pathway is regulated to prevent the futile export of inactive substrate. DmsD is part of a class of cytoplasmic chaperones that play a role in preventing certain redox proteins from premature transport. DmsD from Escherichia coli has been crystallized in space group P4_12_12, with unit-cell parameters a = b = 97.45, c = 210.04 Å, in the presence of a small peptide. The structure has been solved by molecular replacement to a resolution of 2.4 Å and refined to an R factor of 19.4%. There are four molecules in the asymmetric unit that may mimic a higher order structure in vivo. There appears to be density for the peptide in a predicted binding pocket, which lends support to its role as the signal-recognition surface for this class of proteins.

Additional Information

Copyright © 2009 International Union of Crystallography. Received 28 May 2009. Accepted 21 June 2009. We thank A. Müller and D. Rees for discussion and comments on the manuscript. We thank Gordon and Betty Moore for support of the Molecular Observatory at Caltech. All data collection was performed on beamline 9-2 at SSRL. Operations at SSRL are supported by the US DOE and NIH. WMC is supported by awards from the Searle Scholar program and the Burroughs–Wellcome fund career award for biological sciences. PDB Reference: DmsD, 3cw0, r3cw0sf.

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