2VLI

Structure of Deinococcus radiodurans tunicamycin resistance protein

Summary for 2VLI

• Entry DOI: 10.2210/pdb2vli/pdb
• Descriptor: ANTIBIOTIC RESISTANCE PROTEIN, CADMIUM ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: transferase, phosphotransferase
• Biological source: DEINOCOCCUS RADIODURANS
• Total number of polymer chains: 2
• Total formula weight: 40988.89

Authors

Macedo, S.,Kapp, U.,Leiros, I.,Hall, D.R.,Mitchell, E. (deposition date: 2008-01-15, release date: 2008-06-17, Last modification date: 2024-11-13)

Primary citation

Kapp, U.,Macedo, S.,Hall, D.R.,Leiros, I.,Mcsweeney, S.M.,Mitchell, E.
Structure of Deinococcus Radiodurans Tunicamycin-Resistance Protein (Tmrd), a Phosphotransferase.
Acta Crystallogr.,Sect.F, 64:479-, 2008

PubMed Abstract: 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.

PubMed: 18540055
DOI: 10.1107/S1744309108011822

Experimental method

X-RAY DIFFRACTION (1.95 Å)