Structural analysis of a monomeric form of the twin-arginine leader peptide binding chaperone Escherichia coli DmsD.

ABSTRACT: The redox enzyme maturation proteins play an essential role in the proofreading and membrane targeting of protein substrates to the twin-arginine translocase. Functionally, the most thoroughly characterized redox enzyme maturation protein to date is Escherichia coli DmsD (EcDmsD). Herein, we present the X-ray crystal structure of the monomeric form of the EcDmsD refined to 2.0 A resolution, with clear electron density present for each of its 204 amino acid residues. The structural data presented here complement the biochemical data previously generated regarding the function of these twin-arginine translocase leader peptide binding chaperone proteins. Docking and molecular dynamics simulation experiments were used to provide a proposed model for how this chaperone is able to recognize the

SUBMITTER: Stevens CM 

PROVIDER: S-EPMC3285696 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature