Document Detail


Structural analysis of a monomeric form of the twin-arginine leader peptide binding chaperone Escherichia coli DmsD.
MedLine Citation:
PMID:  19361518     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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 leader peptide of its substrate DmsA. The interactions observed in the model are in agreement with previous biochemical data and suggest intimate interactions between the conserved twin-arginine motif of the leader peptide of E. coli DmsA and the most conserved regions on the surface of EcDmsD.
Authors:
Charles M Stevens; Tara M L Winstone; Raymond J Turner; Mark Paetzel
Related Documents :
20712308 - De novo design of peptide-calcite biomineralization systems.
15159558 - Azospirillum irakense pectate lyase displays a toroidal fold.
15299678 - Structure of escherichia coli inorganic pyrophosphatase at 2.2 a resolution.
19361518 - Structural analysis of a monomeric form of the twin-arginine leader peptide binding cha...
15964018 - Restricted variable residues in the c-terminal segment of hiv-1 v3 loop regulate the mo...
6988518 - Adenosine diphosphate-ribosylation of adenylate cyclase catalyzed by heat-labile entero...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-04-08
Journal Detail:
Title:  Journal of molecular biology     Volume:  389     ISSN:  1089-8638     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2009 May 
Date Detail:
Created Date:  2009-05-12     Completed Date:  2009-06-04     Revised Date:  2013-06-02    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  124-33     Citation Subset:  IM    
Affiliation:
Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada.
Data Bank Information
Bank Name/Acc. No.:
PDB/3EFP
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Binding Sites
Carrier Proteins / chemistry*
Computer Simulation
Crystallography, X-Ray
Escherichia coli / chemistry*
Escherichia coli Proteins / chemistry*,  metabolism*
Membrane Transport Proteins / metabolism*
Models, Molecular
Molecular Chaperones / chemistry*
Molecular Sequence Data
Protein Binding
Protein Sorting Signals*
Protein Structure, Secondary
Grant Support
ID/Acronym/Agency:
49422//Canadian Institutes of Health Research
Chemical
Reg. No./Substance:
0/Carrier Proteins; 0/DmsD protein, E coli; 0/Escherichia coli Proteins; 0/Membrane Transport Proteins; 0/Molecular Chaperones; 0/Protein Sorting Signals; 0/twin-arginine translocase complex, E coli
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Two GxxxG-like motifs facilitate promiscuous interactions of the human ErbB transmembrane domains.
Next Document:  Kinetic analysis of the guanine nucleotide exchange activity of TRAPP, a multimeric Ypt1p exchange f...