1xtz
From Proteopedia
(New page: 200px<br /><applet load="1xtz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xtz, resolution 2.10Å" /> '''Crystal structure of...) |
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| - | [[Image:1xtz.gif|left|200px]]<br /><applet load="1xtz" size=" | + | [[Image:1xtz.gif|left|200px]]<br /><applet load="1xtz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xtz, resolution 2.10Å" /> | caption="1xtz, resolution 2.10Å" /> | ||
'''Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archeal and bacterial enzymes'''<br /> | '''Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archeal and bacterial enzymes'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Ribose-5-phosphate isomerase A has an important role in sugar metabolism | + | 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 Structure== | ==About this Structure== | ||
| - | 1XTZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/Ribose-5-phosphate_isomerase Ribose-5-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.6 5.3.1.6] Full crystallographic information is available from [http:// | + | 1XTZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/Ribose-5-phosphate_isomerase Ribose-5-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.6 5.3.1.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XTZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Quevillon-Cheruel, S.]] | [[Category: Quevillon-Cheruel, S.]] | ||
[[Category: Sorel, I.]] | [[Category: Sorel, I.]] | ||
| - | [[Category: Tilbeurgh, H | + | [[Category: Tilbeurgh, H van.]] |
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
[[Category: d-ribose-5-phosphate isomerase]] | [[Category: d-ribose-5-phosphate isomerase]] | ||
[[Category: yeast]] | [[Category: yeast]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:58:36 2008'' |
Revision as of 13:58, 21 February 2008
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Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archeal and bacterial enzymes
Overview
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 Structure
1XTZ is a Single protein structure of sequence from Saccharomyces cerevisiae. Active as Ribose-5-phosphate isomerase, with EC number 5.3.1.6 Full crystallographic information is available from OCA.
Reference
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
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