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[[Image:1e58.gif|left|200px]]
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{{STRUCTURE_1e58|  PDB=1e58  |  SCENE=  }}
'''E.COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE'''


==E.coli cofactor-dependent phosphoglycerate mutase==
<StructureSection load='1e58' size='340' side='right'caption='[[1e58]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1e58]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. The February 2004 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''The Glycolytic Enzymes''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2004_2 10.2210/rcsb_pdb/mom_2004_2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E58 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]] 1.25&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</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=1e58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e58 OCA], [https://pdbe.org/1e58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e58 RCSB], [https://www.ebi.ac.uk/pdbsum/1e58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e58 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GPMA_ECOLI GPMA_ECOLI] Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.[HAMAP-Rule:MF_01039]
== 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/e5/1e58_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=1e58 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The active conformation of the dimeric cofactor-dependent phosphoglycerate mutase (dPGM) from Escherichia coli has been elucidated by crystallographic methods to a resolution of 1.25 A (R-factor 0.121; R-free 0.168). The active site residue His(10), central in the catalytic mechanism of dPGM, is present as a phosphohistidine with occupancy of 0.28. The structural changes on histidine phosphorylation highlight various features that are significant in the catalytic mechanism. The C-terminal 10-residue tail, which is not observed in previous dPGM structures, is well ordered and interacts with residues implicated in substrate binding; the displacement of a loop adjacent to the active histidine brings previously overlooked residues into positions where they may directly influence catalysis. E. coli dPGM, like the mammalian dPGMs, is a dimer, whereas previous structural work has concentrated on monomeric and tetrameric yeast forms. We can now analyze the sequence differences that cause this variation of quaternary structure.


==Overview==
High resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase.,Bond CS, White MF, Hunter WN J Biol Chem. 2001 Feb 2;276(5):3247-53. Epub 2000 Oct 18. PMID:11038361<ref>PMID:11038361</ref>
The active conformation of the dimeric cofactor-dependent phosphoglycerate mutase (dPGM) from Escherichia coli has been elucidated by crystallographic methods to a resolution of 1.25 A (R-factor 0.121; R-free 0.168). The active site residue His(10), central in the catalytic mechanism of dPGM, is present as a phosphohistidine with occupancy of 0.28. The structural changes on histidine phosphorylation highlight various features that are significant in the catalytic mechanism. The C-terminal 10-residue tail, which is not observed in previous dPGM structures, is well ordered and interacts with residues implicated in substrate binding; the displacement of a loop adjacent to the active histidine brings previously overlooked residues into positions where they may directly influence catalysis. E. coli dPGM, like the mammalian dPGMs, is a dimer, whereas previous structural work has concentrated on monomeric and tetrameric yeast forms. We can now analyze the sequence differences that cause this variation of quaternary structure.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1E58 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 1E58 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E58 OCA].
</div>
<div class="pdbe-citations 1e58" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
High resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase., Bond CS, White MF, Hunter WN, J Biol Chem. 2001 Feb 2;276(5):3247-53. Epub 2000 Oct 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11038361 11038361]
*[[Phosphoglycerate mutase 3D structures|Phosphoglycerate mutase 3D structures]]
[[Category: Escherichia coli]]
== References ==
[[Category: Phosphoglycerate mutase]]
<references/>
[[Category: Single protein]]
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: The Glycolytic Enzymes]]
[[Category: The Glycolytic Enzymes]]
[[Category: Bond, C S.]]
[[Category: Bond CS]]
[[Category: Hunter, W N.]]
[[Category: Hunter WN]]
[[Category: Glycolysis and gluconeogenesis]]
[[Category: Isomerase]]
[[Category: Phosphoglycerate mutase]]
[[Category: Phosphohistidine]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:40:41 2008''

Latest revision as of 08:18, 9 April 2025

E.coli cofactor-dependent phosphoglycerate mutase

1e58, resolution 1.25Å

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