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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 9
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pubmed:dateCreated |
2006-9-1
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pubmed:databankReference |
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pubmed:abstractText |
The structure of the NAD-dependent oxidoreductase UDP-galactose-4'-epimerase from Trypanosoma brucei in complex with cofactor and the substrate analogue UDP-4-deoxy-4-fluoro-alpha-D-galactose has been determined using diffraction data to 2.7 A resolution. Despite the high level of sequence and structure conservation between the trypanosomatid enzyme and those from humans, yeast and bacteria, the binding of the 4-fluoro-alpha-D-galactose moiety is distinct from previously reported structures. Of particular note is the observation that when bound to the T. brucei enzyme, the galactose moiety of this fluoro-derivative is rotated approximately 180 degrees with respect to the orientation of the hexose component of UDP-glucose when in complex with the human enzyme. The architecture of the catalytic centre is designed to effectively bind different orientations of the hexose, a finding that is consistent with a mechanism that requires the sugar to maintain a degree of flexibility within the active site.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-10531030,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-10801319,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-11373620,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-11976334,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-11983889,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-12615316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-12631733,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-12686589,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-12923184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-14635134,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-14966133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-15136592,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-15509560,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-15767252,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-16569451,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-7656031,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-8611497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-9174344,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-9217258,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-9271074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946458-9574932
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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 |
Sep
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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 |
62
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
829-34
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16946458-Animals,
pubmed-meshheading:16946458-Catalytic Domain,
pubmed-meshheading:16946458-Crystallography, X-Ray,
pubmed-meshheading:16946458-NAD,
pubmed-meshheading:16946458-Protein Structure, Secondary,
pubmed-meshheading:16946458-Substrate Specificity,
pubmed-meshheading:16946458-Trypanosoma brucei brucei,
pubmed-meshheading:16946458-UDPglucose 4-Epimerase,
pubmed-meshheading:16946458-Uridine Diphosphate Galactose
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pubmed:year |
2006
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pubmed:articleTitle |
Trypanosoma brucei UDP-galactose-4'-epimerase in ternary complex with NAD+ and the substrate analogue UDP-4-deoxy-4-fluoro-alpha-D-galactose.
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pubmed:affiliation |
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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