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PDBsum entry 2vli
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References listed in PDB file
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Key reference
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Title
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Structure of deinococcus radiodurans tunicamycin-Resistance protein (tmrd), A phosphotransferase.
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Authors
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U.Kapp,
S.Macedo,
D.R.Hall,
I.Leiros,
S.M.Mcsweeney,
E.Mitchell.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008,
64,
479-486.
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PubMed id
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Abstract
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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.
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