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[[Image:1e58.gif|left|200px]]<br />
<applet load="1e58" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1e58, resolution 1.25&Aring;" />
'''E.COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE'''<br />


==Overview==
==E.coli cofactor-dependent phosphoglycerate mutase==
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.
<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/initialview01.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>


==About this Structure==
==See Also==
1E58 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and CL as [http://en.wikipedia.org/wiki/ligands ligands]. 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]]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] Structure known Active Site: HIS. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E58 OCA].
*[[Phosphoglycerate mutase 3D structures|Phosphoglycerate mutase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11038361 11038361]
[[Category: Escherichia coli K-12]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Phosphoglycerate mutase]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Single protein]]
[[Category: The Glycolytic Enzymes]]
[[Category: The Glycolytic Enzymes]]
[[Category: Bond, C.S.]]
[[Category: Bond CS]]
[[Category: Hunter, W.N.]]
[[Category: Hunter WN]]
[[Category: CL]]
[[Category: SO4]]
[[Category: glycolysis and gluconeogenesis]]
[[Category: isomerase]]
[[Category: phosphoglycerate mutase]]
[[Category: phosphohistidine]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 12:49:25 2007''

Latest revision as of 12:58, 20 March 2024

E.coli cofactor-dependent phosphoglycerate mutaseE.coli cofactor-dependent phosphoglycerate mutase

Structural highlights

1e58 is a 1 chain structure with sequence from Escherichia coli K-12. The February 2004 RCSB PDB Molecule of the Month feature on The Glycolytic Enzymes by David S. Goodsell is 10.2210/rcsb_pdb/mom_2004_2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.25Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GPMA_ECOLI Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.[HAMAP-Rule:MF_01039]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1e58, resolution 1.25Å

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