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Structure paper

TitleStructural analysis of a monomeric form of the twin-arginine leader peptide binding chaperone Escherichia coli DmsD.
Journal, issue, pagesJ. Mol. Biol., Vol. 389, Page 124-133, Year 2009
Publish dateSep 9, 2008 (structure data deposition date)
AuthorsStevens, C.M. / Winstone, T.M. / Turner, R.J. / Paetzel, M.
External linksJ. Mol. Biol. / PubMed:19361518
MethodsX-ray diffraction
Resolution2.01 Å
Structure data

PDB-3efp:
Crystal structure of the Escherichia coli twin arginine leader peptide binding protein DmsD in a monomeric form
Method: X-RAY DIFFRACTION / Resolution: 2.01 Å

Chemicals

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-GOL:
GLYCEROL

ChemComp-CL:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsCHAPERONE / twin-arginine translocation (Tat) / protein targeting / protein translocation / leader peptide / signal peptide / redox enzyme maturation protein (REMP)

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