1xtz: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1xtz.gif|left|200px]] | [[Image:1xtz.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1xtz", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_1xtz| PDB=1xtz | SCENE= }} | |||
}} | |||
'''Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archeal and bacterial enzymes''' | '''Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archeal and bacterial enzymes''' | ||
Line 33: | Line 30: | ||
[[Category: Sorel, I.]] | [[Category: Sorel, I.]] | ||
[[Category: Tilbeurgh, H van.]] | [[Category: Tilbeurgh, H van.]] | ||
[[Category: | [[Category: Crystal structure]] | ||
[[Category: | [[Category: D-ribose-5-phosphate isomerase]] | ||
[[Category: | [[Category: Yeast]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:30:15 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 15:30, 3 May 2008
Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archeal and bacterial enzymes
OverviewOverview
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.
About this StructureAbout this Structure
1XTZ is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archaeal and bacterial enzymes., Graille M, Meyer P, Leulliot N, Sorel I, Janin J, Van Tilbeurgh H, Quevillon-Cheruel S, Biochimie. 2005 Aug;87(8):763-9. Epub 2005 Apr 5. PMID:16054529 Page seeded by OCA on Sat May 3 15:30:15 2008