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[[Image:5pgm.gif|left|200px]]
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{{STRUCTURE_5pgm|  PDB=5pgm  |  SCENE=  }}
'''SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE'''


==SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE==
<StructureSection load='5pgm' size='340' side='right'caption='[[5pgm]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5pgm]] is a 8 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=5PGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5PGM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.12&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5pgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5pgm OCA], [https://pdbe.org/5pgm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5pgm RCSB], [https://www.ebi.ac.uk/pdbsum/5pgm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5pgm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PMG1_YEAST PMG1_YEAST] Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also Catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pg/5pgm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=5pgm ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of a new crystal form of Saccharomyces cerevisiae phosphoglycerate mutase has been solved and refined to 2.12 A with working and free R-factors of 19.7 and 22.9 %, respectively. Higher-resolution data and greater non-crystallographic symmetry have produced a more accurate protein structure than previously. Prominent among the differences from the previous structure is the presence of two sulphate ions within each active site cleft. The separation of the sulphates suggests that they may occupy the same sites as phospho groups of the bisphosphate ligands of the enzyme. Plausible binding modes for 2,3-bisphosphoglycerate and 1, 3-bisphosphoglycerate are thereby suggested. These results support previous conclusions from mutant studies, highlight interesting new targets for mutagenesis and suggest a possible mechanism of enzyme phosphorylation.


==Overview==
Sulphate ions observed in the 2.12 A structure of a new crystal form of S. cerevisiae phosphoglycerate mutase provide insights into understanding the catalytic mechanism.,Rigden DJ, Walter RA, Phillips SE, Fothergill-Gilmore LA J Mol Biol. 1999 Mar 12;286(5):1507-17. PMID:10064712<ref>PMID:10064712</ref>
The structure of a new crystal form of Saccharomyces cerevisiae phosphoglycerate mutase has been solved and refined to 2.12 A with working and free R-factors of 19.7 and 22.9 %, respectively. Higher-resolution data and greater non-crystallographic symmetry have produced a more accurate protein structure than previously. Prominent among the differences from the previous structure is the presence of two sulphate ions within each active site cleft. The separation of the sulphates suggests that they may occupy the same sites as phospho groups of the bisphosphate ligands of the enzyme. Plausible binding modes for 2,3-bisphosphoglycerate and 1, 3-bisphosphoglycerate are thereby suggested. These results support previous conclusions from mutant studies, highlight interesting new targets for mutagenesis and suggest a possible mechanism of enzyme phosphorylation.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
5PGM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5PGM OCA].
</div>
<div class="pdbe-citations 5pgm" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Sulphate ions observed in the 2.12 A structure of a new crystal form of S. cerevisiae phosphoglycerate mutase provide insights into understanding the catalytic mechanism., Rigden DJ, Walter RA, Phillips SE, Fothergill-Gilmore LA, J Mol Biol. 1999 Mar 12;286(5):1507-17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10064712 10064712]
*[[Bromodomain adjacent to zinc finger 3D structures|Bromodomain adjacent to zinc finger 3D structures]]
[[Category: Phosphoglycerate mutase]]
*[[Phosphoglycerate mutase 3D structures|Phosphoglycerate mutase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Fothergill-Gilmore LA]]
[[Category: Fothergill-Gilmore, L A.]]
[[Category: Phillips SEV]]
[[Category: Phillips, S E.V.]]
[[Category: Rigden DJ]]
[[Category: Rigden, D J.]]
[[Category: Glycolytic enzyme]]
[[Category: Isomerase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:37:00 2008''

Latest revision as of 09:52, 25 December 2024

SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE

5pgm, resolution 2.12Å

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