3EFP
Crystal structure of the Escherichia coli twin arginine leader peptide binding protein DmsD in a monomeric form
Summary for 3EFP
| Entry DOI | 10.2210/pdb3efp/pdb |
| Descriptor | Twin-arginine leader-binding protein dmsD, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | twin-arginine translocation (tat), protein targeting, protein translocation, chaperone, leader peptide, signal peptide, redox enzyme maturation protein (remp) |
| Biological source | Escherichia coli |
| Cellular location | Cell inner membrane; Peripheral membrane protein: P69853 |
| Total number of polymer chains | 2 |
| Total formula weight | 48978.95 |
| Authors | Stevens, C.M.,Paetzel, M. (deposition date: 2008-09-09, release date: 2009-04-07, Last modification date: 2023-08-30) |
| Primary citation | Stevens, C.M.,Winstone, T.M.,Turner, R.J.,Paetzel, M. Structural analysis of a monomeric form of the twin-arginine leader peptide binding chaperone Escherichia coli DmsD. J.Mol.Biol., 389:124-133, 2009 Cited by PubMed 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 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. PubMed: 19361518DOI: 10.1016/j.jmb.2009.03.069 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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