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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 6
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pubmed:dateCreated |
2008-6-9
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pubmed:abstractText |
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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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18540055-101533,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18540055-10320398,
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1744-3091
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
64
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
479-86
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pubmed:dateRevised |
2010-9-21
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pubmed:meshHeading |
pubmed-meshheading:18540055-Adenosine Triphosphate,
pubmed-meshheading:18540055-Amino Acid Sequence,
pubmed-meshheading:18540055-Anti-Bacterial Agents,
pubmed-meshheading:18540055-Bacterial Proteins,
pubmed-meshheading:18540055-Crystallography, X-Ray,
pubmed-meshheading:18540055-Deinococcus,
pubmed-meshheading:18540055-Genome, Bacterial,
pubmed-meshheading:18540055-Hydrogen Bonding,
pubmed-meshheading:18540055-Models, Molecular,
pubmed-meshheading:18540055-Molecular Sequence Data,
pubmed-meshheading:18540055-Molecular Structure,
pubmed-meshheading:18540055-Open Reading Frames,
pubmed-meshheading:18540055-Phosphotransferases,
pubmed-meshheading:18540055-Protein Structure, Secondary,
pubmed-meshheading:18540055-Protein Structure, Tertiary,
pubmed-meshheading:18540055-Sequence Homology, Amino Acid,
pubmed-meshheading:18540055-Spectrum Analysis, Raman,
pubmed-meshheading:18540055-Tunicamycin,
pubmed-meshheading:18540055-Water
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pubmed:year |
2008
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pubmed:articleTitle |
Structure of Deinococcus radiodurans tunicamycin-resistance protein (TmrD), a phosphotransferase.
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pubmed:affiliation |
European Synchrotron Radiation Facility, 6 Rue Jules Horowitz, BP-220, 38043 Grenoble, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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