|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
23
|
|
pubmed:dateCreated |
2008-6-2
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
The glycosyltransferase termed MshA catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to 1-L-myo-inositol-1-phosphate in the first committed step of mycothiol biosynthesis. The structure of MshA from Corynebacterium glutamicum was determined both in the absence of substrates and in a complex with UDP and 1-L-myo-inositol-1-phosphate. MshA belongs to the GT-B structural family whose members have a two-domain structure with both domains exhibiting a Rossman-type fold. Binding of the donor sugar to the C-terminal domain produces a 97 degrees rotational reorientation of the N-terminal domain relative to the C-terminal domain, clamping down on UDP and generating the binding site for 1-L-myo-inositol-1-phosphate. The structure highlights the residues important in binding of UDP-N-acetylglucosamine and 1-L-myo-inositol-1-phosphate. Molecular models of the ternary complex suggest a mechanism in which the beta-phosphate of the substrate, UDP-N-acetylglucosamine, promotes the nucleophilic attack of the 3-hydroxyl group of 1-L-myo-inositol-1-phosphate while at the same time promoting the cleavage of the sugar nucleotide bond.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-10570792,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-11015222,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-11092856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-11175908,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-11518970,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-11785761,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-12033919,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-12146938,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-12375100,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-12384335,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-12420157,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-12498887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-12538870,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-12691742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-12754249,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-12874381,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-12948636,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-12958317,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-14570926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-14594852,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-15075344,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-15081655,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-15272157,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-15272305,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-15299911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-15299926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-15572765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-15730267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-16049187,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-16237013,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-16326705,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-16369093,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-16369096,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-16923891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-16940050,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-17020551,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-17113996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-17165744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-17347437,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-17510062,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-18046457,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-18205830,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-3134344,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-3143309,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-7798231,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-8606174,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-9020780,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18390549-9804803
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jun
|
|
pubmed:issn |
0021-9258
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
6
|
|
pubmed:volume |
283
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
15834-44
|
|
pubmed:dateRevised |
2010-9-22
|
|
pubmed:meshHeading |
pubmed-meshheading:18390549-Acetylglucosamine,
pubmed-meshheading:18390549-Binding Sites,
pubmed-meshheading:18390549-Catalysis,
pubmed-meshheading:18390549-Corynebacterium glutamicum,
pubmed-meshheading:18390549-Glycosyltransferases,
pubmed-meshheading:18390549-Inositol Phosphates,
pubmed-meshheading:18390549-Models, Molecular,
pubmed-meshheading:18390549-Protein Folding,
pubmed-meshheading:18390549-Protein Structure, Tertiary,
pubmed-meshheading:18390549-Structural Homology, Protein,
pubmed-meshheading:18390549-Uridine Diphosphate
|
|
pubmed:year |
2008
|
|
pubmed:articleTitle |
Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: substrate-assisted catalysis.
|
|
pubmed:affiliation |
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA. vetting@aecom.yu.edu
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|
