Source:http://linkedlifedata.com/resource/pubmed/id/16054529
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
8
|
| pubmed:dateCreated |
2005-8-1
|
| pubmed:databankReference | |
| pubmed:abstractText |
Ribose-5-phosphate isomerase A has an important role in sugar metabolism by interconverting ribose-5-phosphate and ribulose-5-phosphate. This enzyme is ubiquitous and highly conserved among the three kingdoms of life. We have solved the 2.1 A resolution crystal structure of the Saccharomyces cerevisiae enzyme by molecular replacement. This protein adopts the same fold as its archaeal and bacterial orthologs with two alpha/beta domains tightly packed together. Mapping of conserved residues at the surface of the protein reveals strong invariability of the active site pocket, suggesting a common ligand binding mode and a similar catalytic mechanism. The yeast enzyme associates as a homotetramer similarly to the archaeal protein. The effect of an inactivating mutation (Arg189 to Lys) is discussed in view of the information brought by this structure.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0300-9084
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
87
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
763-9
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| pubmed:dateRevised |
2011-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:16054529-Aldose-Ketose Isomerases,
pubmed-meshheading:16054529-Amino Acid Sequence,
pubmed-meshheading:16054529-Archaea,
pubmed-meshheading:16054529-Bacteria,
pubmed-meshheading:16054529-Binding Sites,
pubmed-meshheading:16054529-Catalysis,
pubmed-meshheading:16054529-Cloning, Molecular,
pubmed-meshheading:16054529-Crystallography, X-Ray,
pubmed-meshheading:16054529-Models, Molecular,
pubmed-meshheading:16054529-Molecular Sequence Data,
pubmed-meshheading:16054529-Mutation,
pubmed-meshheading:16054529-Protein Conformation,
pubmed-meshheading:16054529-Protein Folding,
pubmed-meshheading:16054529-Protein Structure, Secondary,
pubmed-meshheading:16054529-Protein Structure, Tertiary,
pubmed-meshheading:16054529-Ribulosephosphates,
pubmed-meshheading:16054529-Saccharomyces cerevisiae,
pubmed-meshheading:16054529-Sequence Alignment,
pubmed-meshheading:16054529-Sequence Homology, Amino Acid
|
| pubmed:year |
2005
|
| pubmed:articleTitle |
Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archaeal and bacterial enzymes.
|
| pubmed:affiliation |
Institut de Biochimie et de Biophysique Moléculaire et Cellulaire, CNRS-UMR 8619, Université Paris-Sud, Bâtiment 430, 91405 Orsay, France.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|