Structural highlights
3u41 is a 8 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | X-ray diffraction, Resolution 2.5Å |
| Ligands: | CL, GOL, PEG, SO4, TRS |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
DMSD_ECOLI Required for biogenesis/assembly of DMSO reductase, but not for the interaction of the DmsA signal peptide with the Tat system. May be part of a chaperone cascade complex that facilitates a folding-maturation pathway for the substrate protein.[1] [2] [3] [4]
References
- ↑ Oresnik IJ, Ladner CL, Turner RJ. Identification of a twin-arginine leader-binding protein. Mol Microbiol. 2001 Apr;40(2):323-31. PMID:11309116
- ↑ Ray N, Oates J, Turner RJ, Robinson C. DmsD is required for the biogenesis of DMSO reductase in Escherichia coli but not for the interaction of the DmsA signal peptide with the Tat apparatus. FEBS Lett. 2003 Jan 16;534(1-3):156-60. PMID:12527378
- ↑ Papish AL, Ladner CL, Turner RJ. The twin-arginine leader-binding protein, DmsD, interacts with the TatB and TatC subunits of the Escherichia coli twin-arginine translocase. J Biol Chem. 2003 Aug 29;278(35):32501-6. Epub 2003 Jun 17. PMID:12813051 doi:https://dx.doi.org/10.1074/jbc.M301076200
- ↑ Li H, Chang L, Howell JM, Turner RJ. DmsD, a Tat system specific chaperone, interacts with other general chaperones and proteins involved in the molybdenum cofactor biosynthesis. Biochim Biophys Acta. 2010 Jun;1804(6):1301-9. doi: 10.1016/j.bbapap.2010.01.022., Epub 2010 Feb 11. PMID:20153451 doi:https://dx.doi.org/10.1016/j.bbapap.2010.01.022
