Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The open-reading frame (ORF) DR_1419 in the Deinococcus radiodurans genome is annotated as a representative of the wide family of tunicamycin-resistance proteins as identified in a range of bacterial genomes. The D. radiodurans ORF DR_1419 was cloned and expressed; the protein TmrD was crystallized and its X-ray crystal structure was determined to 1.95 A resolution. The structure was determined using single-wavelength anomalous diffraction with selenomethionine-derivatized protein. The refined structure is the first to be reported for a member of the tunicamycin-resistance family. It reveals strong structural similarity to the family of nucleoside monophosphate kinases and to the chloramphenicol phosphotransferase of Streptomyces venezuelae, suggesting that the mode of action is possibly by phosphorylation of tunicamycin.
Structure of Deinococcus radiodurans tunicamycin-resistance protein (TmrD), a phosphotransferase.,Kapp U, Macedo S, Hall DR, Leiros I, McSweeney SM, Mitchell E Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jun 1;64(Pt 6):479-86., Epub 2008 May 16. PMID:18540055[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kapp U, Macedo S, Hall DR, Leiros I, McSweeney SM, Mitchell E. Structure of Deinococcus radiodurans tunicamycin-resistance protein (TmrD), a phosphotransferase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jun 1;64(Pt 6):479-86., Epub 2008 May 16. PMID:18540055 doi:10.1107/S1744309108011822
