Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archaeal and bacterial enzymes
| Autor: | M, Graille, P, Meyer, N, Leulliot, I, Sorel, J, Janin, H, Van Tilbeurgh, S, Quevillon-Cheruel |
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| Rok vydání: | 2004 |
| Předmět: |
Models
Molecular Protein Folding Binding Sites Bacteria Sequence Homology Amino Acid Protein Conformation Molecular Sequence Data Saccharomyces cerevisiae Crystallography X-Ray Archaea Catalysis Protein Structure Secondary Protein Structure Tertiary Ribulosephosphates Mutation Amino Acid Sequence Cloning Molecular Sequence Alignment Aldose-Ketose Isomerases |
| Zdroj: | Biochimie. 87(8) |
| ISSN: | 0300-9084 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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