3CW0
E.coli DmsD
Summary for 3CW0
| Entry DOI | 10.2210/pdb3cw0/pdb |
| Descriptor | Twin-arginine leader-binding protein dmsD (2 entities in total) |
| Functional Keywords | dmsd, alpha-helices, chaperone, membrane |
| Biological source | Escherichia coli K-12 |
| Cellular location | Cell inner membrane ; Peripheral membrane protein : P69853 |
| Total number of polymer chains | 4 |
| Total formula weight | 94887.46 |
| Authors | Ramasamy, S.,Clemons, W. (deposition date: 2008-04-21, release date: 2009-04-28, Last modification date: 2024-02-21) |
| Primary citation | Ramasamy, S.K.,Clemons, W.M. Structure of the twin-arginine signal-binding protein DmsD from Escherichia coli. Acta Crystallogr.,Sect.F, 65:746-750, 2009 Cited by PubMed Abstract: 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 P4(1)2(1)2, with unit-cell parameters a = b = 97.45, c = 210.04 A, in the presence of a small peptide. The structure has been solved by molecular replacement to a resolution of 2.4 A 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. PubMed: 19652330DOI: 10.1107/S1744309109023811 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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