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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3-4
|
| pubmed:dateCreated |
1997-8-15
|
| pubmed:abstractText |
The three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana has been solved at 2.2 A resolution (Reinemer et al., 1996). The enzyme forms a dimer of two identical subunits. The structure shows a new G-site architecture and a novel and unique dimer interface. Each monomer of the protein forms a separate G-site. Therefore, the requirements on the dimer interface are reduced. As a consequence, the interactions between the monomers are weaker and residues at the dimer interface are more variable. Thus, the dimer interface looses its relevance for a classification of plant glutathione S-transferases and the formation of heterodimers becomes even more difficult to predict.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
1431-6730
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
378
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
317-20
|
| pubmed:dateRevised |
2000-12-18
|
| pubmed:meshHeading |
pubmed-meshheading:9165087-Amino Acid Sequence,
pubmed-meshheading:9165087-Binding Sites,
pubmed-meshheading:9165087-Glutathione,
pubmed-meshheading:9165087-Glutathione Transferase,
pubmed-meshheading:9165087-Models, Molecular,
pubmed-meshheading:9165087-Molecular Sequence Data,
pubmed-meshheading:9165087-Plants
|
| pubmed:articleTitle |
Dimer interface of glutathione S-transferase from Arabidopsis thaliana: influence of the G-site architecture on the dimer interface and implications for classification.
|
| pubmed:affiliation |
Max-Planck-Institut für Biochemie, Abt. Strukturforschung, Martinsried, Germany.
|
| pubmed:publicationType |
Journal Article
|