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| | <StructureSection load='2cis' size='340' side='right'caption='[[2cis]], [[Resolution|resolution]] 1.62Å' scene=''> | | <StructureSection load='2cis' size='340' side='right'caption='[[2cis]], [[Resolution|resolution]] 1.62Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2cis]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CIS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CIS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2cis]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CIS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CIS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=TA6:6-O-PHOSPHONO-BETA-D-TAGATOFURANOSE'>TA6</scene></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]] 1.62Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=TA6:6-O-PHOSPHONO-BETA-D-TAGATOFURANOSE'>TA6</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ciq|2ciq]], [[2cir|2cir]]</div></td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glucose-6-phosphate_1-epimerase Glucose-6-phosphate 1-epimerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.15 5.1.3.15] </span></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=2cis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cis OCA], [https://pdbe.org/2cis PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cis RCSB], [https://www.ebi.ac.uk/pdbsum/2cis PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cis ProSAT]</span></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=2cis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cis OCA], [https://pdbe.org/2cis PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cis RCSB], [https://www.ebi.ac.uk/pdbsum/2cis PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cis ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/YMY9_YEAST YMY9_YEAST]] Catalyzes the interconversion between the alpha and beta anomers from at least three hexose 6-phosphate sugars (Glc6P, Gal6P, and Man6P).<ref>PMID:16857670</ref>
| + | [https://www.uniprot.org/uniprot/YMY9_YEAST YMY9_YEAST] Catalyzes the interconversion between the alpha and beta anomers from at least three hexose 6-phosphate sugars (Glc6P, Gal6P, and Man6P).<ref>PMID:16857670</ref> |
| | == 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: Baker's yeast]] | |
| - | [[Category: Glucose-6-phosphate 1-epimerase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Baltaze, J P]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Graille, M]] | + | [[Category: Baltaze J-P]] |
| - | [[Category: Leulliot, N]] | + | [[Category: Graille M]] |
| - | [[Category: Liger, D]] | + | [[Category: Leulliot N]] |
| - | [[Category: Quevillon-Cheruel, S]] | + | [[Category: Liger D]] |
| - | [[Category: Tilbeurgh, H van]] | + | [[Category: Quevillon-Cheruel S]] |
| - | [[Category: Galactose-6-phosphate-1-epimerase]]
| + | [[Category: Van Tilbeurgh H]] |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Mannose-6-phosphate-1-epimerase]]
| + | |
| Structural highlights
Function
YMY9_YEAST Catalyzes the interconversion between the alpha and beta anomers from at least three hexose 6-phosphate sugars (Glc6P, Gal6P, and Man6P).[1]
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
Despite the generation of a large amount of sequence information over the last decade, more than 40% of well characterized enzymatic functions still lack associated protein sequences. Assigning protein sequences to documented biochemical functions is an interesting challenge. We illustrate here that structural genomics may be a reasonable approach in addressing these questions. We present the crystal structure of the Saccharomyces cerevisiae YMR099cp, a protein of unknown function. YMR099cp adopts the same fold as galactose mutarotase and shares the same catalytic machinery necessary for the interconversion of the alpha and beta anomers of galactose. The structure revealed the presence in the active site of a sulfate ion attached by an arginine clamp made by the side chain from two strictly conserved arginine residues. This sulfate is ideally positioned to mimic the phosphate group of hexose 6-phosphate. We have subsequently successfully demonstrated that YMR099cp is a hexose-6-phosphate mutarotase with broad substrate specificity. We solved high resolution structures of some substrate enzyme complexes, further confirming our functional hypothesis. The metabolic role of a hexose-6-phosphate mutarotase is discussed. This work illustrates that structural information has been crucial to assign YMR099cp to the orphan EC activity: hexose-phosphate mutarotase.
Structure-based functional annotation: yeast ymr099c codes for a D-hexose-6-phosphate mutarotase.,Graille M, Baltaze JP, Leulliot N, Liger D, Quevillon-Cheruel S, van Tilbeurgh H J Biol Chem. 2006 Oct 6;281(40):30175-85. Epub 2006 Jul 20. PMID:16857670[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Graille M, Baltaze JP, Leulliot N, Liger D, Quevillon-Cheruel S, van Tilbeurgh H. Structure-based functional annotation: yeast ymr099c codes for a D-hexose-6-phosphate mutarotase. J Biol Chem. 2006 Oct 6;281(40):30175-85. Epub 2006 Jul 20. PMID:16857670 doi:10.1074/jbc.M604443200
- ↑ Graille M, Baltaze JP, Leulliot N, Liger D, Quevillon-Cheruel S, van Tilbeurgh H. Structure-based functional annotation: yeast ymr099c codes for a D-hexose-6-phosphate mutarotase. J Biol Chem. 2006 Oct 6;281(40):30175-85. Epub 2006 Jul 20. PMID:16857670 doi:10.1074/jbc.M604443200
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