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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
|
pubmed:dateCreated |
1995-2-14
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pubmed:abstractText |
We report here the x-ray studies of the complex cytosolic aspartate aminotransferase from chicken heart with D-aspartate at 2,7 A resolution. Crystals of the complex was prepared by diffusing D-aspartate into free enzyme crystals; their space group is P 2(1)2(1)2(1) with cell dimensions (A): a = 62.59; b = 117.83; c = 124.38. They contain one dimeric molecule in the asymmetric unit. The x-ray crystallographic analysis proves that the connection of the D-aspartate induces small conformational changes in the active site of two subunits of the enzyme: considerable conformational changes are determined for His 189, Phe 360, Tyr 70, Arg 292, Phe 18 and Glu 141.
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pubmed:language |
rus
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0006-3029
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
39
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
761-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7819305-Animals,
pubmed-meshheading:7819305-Aspartate Aminotransferases,
pubmed-meshheading:7819305-Aspartic Acid,
pubmed-meshheading:7819305-Binding Sites,
pubmed-meshheading:7819305-Chickens,
pubmed-meshheading:7819305-Crystallography, X-Ray,
pubmed-meshheading:7819305-Myocardium,
pubmed-meshheading:7819305-Protein Conformation
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pubmed:articleTitle |
[The complex of aspartate aminotransferase with D-aspartate].
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pubmed:publicationType |
Journal Article,
English Abstract
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