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| | <StructureSection load='1xtz' size='340' side='right'caption='[[1xtz]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='1xtz' size='340' side='right'caption='[[1xtz]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1xtz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XTZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XTZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1xtz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XTZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XTZ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1lk5|1lk5]], [[1o8b|1o8b]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RKI1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xtz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xtz OCA], [https://pdbe.org/1xtz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xtz RCSB], [https://www.ebi.ac.uk/pdbsum/1xtz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xtz ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1xtz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xtz OCA], [http://pdbe.org/1xtz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xtz RCSB], [http://www.ebi.ac.uk/pdbsum/1xtz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xtz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/RPIA_YEAST RPIA_YEAST] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ribose-5-phosphate isomerase]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Graille, M]] | + | [[Category: Graille M]] |
| - | [[Category: Janin, J]] | + | [[Category: Janin J]] |
| - | [[Category: Leulliot, N]] | + | [[Category: Leulliot N]] |
| - | [[Category: Meyer, P]] | + | [[Category: Meyer P]] |
| - | [[Category: Quevillon-Cheruel, S]] | + | [[Category: Quevillon-Cheruel S]] |
| - | [[Category: Sorel, I]] | + | [[Category: Sorel I]] |
| - | [[Category: Tilbeurgh, H van]] | + | [[Category: Van Tilbeurgh H]] |
| - | [[Category: D-ribose-5-phosphate isomerase]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Yeast]]
| + | |
| Structural highlights
Function
RPIA_YEAST
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. 2005 Aug;87(8):763-9. Epub 2005 Apr 5. PMID:16054529 doi:http://dx.doi.org/10.1016/j.biochi.2005.03.001
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