Linked Life Data

10377386

Source:http://linkedlifedata.com/resource/pubmed/id/10377386

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1999-7-19
pubmed:databankReference
pubmed:abstractText
3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) reductase is the rate-limiting enzyme and the first committed step in the biosynthesis of cholesterol in mammals. We have determined the crystal structures of two nonproductive ternary complexes of HMG-CoA reductase, HMG-CoA/NAD+ and mevalonate/NADH, at 2.8 A resolution. In the structure of the Pseudomonas mevalonii apoenzyme, the last 50 residues of the C terminus (the flap domain), including the catalytic residue His381, were not visible. The structures of the ternary complexes reported here reveal a substrate-induced closing of the flap domain that completes the active site and aligns the catalytic histidine proximal to the thioester of HMG-CoA. The structures also present evidence that Lys267 is critically involved in catalysis and provide insights into the catalytic mechanism.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/10377386-1464741, http://linkedlifedata.com/resource/pubmed/commentcorrection/10377386-15299306, http://linkedlifedata.com/resource/pubmed/commentcorrection/10377386-1634543, http://linkedlifedata.com/resource/pubmed/commentcorrection/10377386-2123872, http://linkedlifedata.com/resource/pubmed/commentcorrection/10377386-4289807, http://linkedlifedata.com/resource/pubmed/commentcorrection/10377386-4395214, http://linkedlifedata.com/resource/pubmed/commentcorrection/10377386-6783074, http://linkedlifedata.com/resource/pubmed/commentcorrection/10377386-7792601, http://linkedlifedata.com/resource/pubmed/commentcorrection/10377386-7908908, http://linkedlifedata.com/resource/pubmed/commentcorrection/10377386-8347566, http://linkedlifedata.com/resource/pubmed/commentcorrection/10377386-8473286, http://linkedlifedata.com/resource/pubmed/commentcorrection/10377386-8810898
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
96
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7167-71
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Substrate-induced closure of the flap domain in the ternary complex structures provides insights into the mechanism of catalysis by 3-hydroxy-3-methylglutaryl-CoA reductase.
pubmed:affiliation
Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't