Linked Life Data

8183265

Source:http://linkedlifedata.com/resource/pubmed/id/8183265

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-6-10
pubmed:abstractText
We report here the first X-ray studies of the complex of cytosolic aspartate aminotransferase from chicken heart with D-aspartate at 2.5 A resolution. Crystals of the complex were grown by cocrystallization (space group is P2(1)2(1)2(1), parameters: a = 62.48 A, b = 117.71 A, c = 124.38 A). They contain one dimeric molecule in the asymmetric unit. The X-ray analysis proves that attachment of D-aspartate induces considerable conformational changes in the active sites of two subunits of the enzyme: both subunits of the complex are in the closed conformation, the interaction of the enzyme with D-aspartate induces a substantial turn (about 90 degrees) of the coenzyme in one subunit, the coenzyme ring is deformed, considerable conformational changes are determined for Phe-18 and Glu-141. Apparently, the amino group of the substrate is a trigger of the conformational changes in the active site of the enzyme.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0026-8984
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
333-41
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
[Study of crystals of aspartate aminotransferase complexed with D-aspartate].
pubmed:publicationType
Journal Article, English Abstract