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Structure of Deinococcus radiodurans tunicamycin-resistance protein (TmrD), a phosphotransferase.


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.

SUBMITTER: Kapp U 

PROVIDER: S-EPMC2496873 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature

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Structure of Deinococcus radiodurans tunicamycin-resistance protein (TmrD), a phosphotransferase.

Kapp Ulrike U   Macedo Sofia S   Hall David Richard DR   Leiros Ingar I   McSweeney Sean M SM   Mitchell Edward E  

Acta crystallographica. Section F, Structural biology and crystallization communications 20080516 Pt 6


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 s  ...[more]

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