Open AccessStructure of the twin‐arginine signal‐binding protein DmsD from Escherichia coli
Author(s) -
Ramasamy Suresh Kumar,
Clemons William M.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109023811
Subject(s) - escherichia coli , signal peptide , chromosomal translocation , arginine , peptide , biochemistry , cytoplasm , chemistry , biophysics , twin arginine translocation pathway , biology , crystallography , peptide sequence , microbiology and biotechnology , amino acid , gene
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 P 4 1 2 1 2, 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.