1XTZ

Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archeal and bacterial enzymes

Summary for 1XTZ

• Entry DOI: 10.2210/pdb1xtz/pdb
• Related: 1LK5 1O8B
• Descriptor: Ribose-5-phosphate isomerase (2 entities in total)
• Functional Keywords: d-ribose-5-phosphate isomerase, yeast, isomerase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 29123.95

Authors

Graille, M.,Meyer, P.,Leulliot, N.,Sorel, I.,Janin, J.,van Tilbeurgh, H.,Quevillon-Cheruel, S. (deposition date: 2004-10-25, release date: 2005-08-30, Last modification date: 2023-08-23)

Primary citation

Graille, M.,Meyer, P.,Leulliot, N.,Sorel, I.,Janin, J.,Van Tilbeurgh, H.,Quevillon-Cheruel, S.
Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archaeal and bacterial enzymes
Biochimie, 87:763-769, 2005

PubMed Abstract: 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: 16054529
DOI: 10.1016/j.biochi.2005.03.001

Experimental method

X-RAY DIFFRACTION (2.1 Å)