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New page: left|200px<br /><applet load="1ebg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ebg, resolution 2.1Å" /> '''CHELATION OF SER 39 T...
 
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[[Image:1ebg.gif|left|200px]]<br /><applet load="1ebg" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ebg, resolution 2.1&Aring;" />
'''CHELATION OF SER 39 TO MG2+ LATCHES A GATE AT THE ACTIVE SITE OF ENOLASE: STRUCTURE OF THE BIS(MG2+) COMPLEX OF YEAST ENOLASE AND THE INTERMEDIATE ANALOG PHOSPHONOACETOHYDROXAMATE AT 2.1 ANGSTROMS RESOLUTION'''<br />


==Overview==
==CHELATION OF SER 39 TO MG2+ LATCHES A GATE AT THE ACTIVE SITE OF ENOLASE: STRUCTURE OF THE BIS(MG2+) COMPLEX OF YEAST ENOLASE AND THE INTERMEDIATE ANALOG PHOSPHONOACETOHYDROXAMATE AT 2.1 ANGSTROMS RESOLUTION==
The structure of a new crystal form of enolase from bakers' yeast has been, solved to 2.1-A resolution. Crystals were grown from poly(ethylene glycol), and KCl at pH 8.2 in the presence of Mg2+ and a reaction intermediate, analog, phosphonoacetohydroxamate (PhAH). Crystals belong to space group, C2; have unit cell dimensions a = 123.5 A, b = 73.9 A, and c = 94.8 A with, beta = 93.3 degrees; and contain one dimer per asymmetric unit. The, structure was solved by molecular replacement from the X-ray coordinates, of apoenolase [Stec, B., &amp; Lebioda, L. (1990) J. Mol. Biol. 211, 235-248]., Both essential divalent metal ions are observed to be complexed with the, inhibitor. The two Mg2+ ions are 4.05 A apart and are bridged by a mu-oxyl, ligand from the carbonyl moiety of PhAH. The "high-affinity" Mg2+, coordinates to the carboxylate side chains of Asp 246, Glu 295, and Asp, 320, one water molecule, and the hydroxamate and carbonyl oxygens of PhAH., The second Mg2+ coordinates to a phosphonyl oxygen, two water molecules, and the mu-bridge carbonyl oxygen of PhAH. Coordination schemes with, respect to PhAH and water ligands are fully consistent with those of the, Mn2+ complexes determined spectroscopically [Poyner, R.R., &amp; Reed, G. H., (1992) Biochemistry 31, 7166-7173]. Remaining ligands for the second Mg2+, are the carbonyl oxygen and gamma-oxygen of Ser 39. Chelation of this Ser, residue to Mg2+ effectively "latches" a flexible loop extending from Gly, 37 through His 43 and closes off the entrance to the active site. The, position of the second Mg2+ in the active site provides new insight into, the stereochemistry of substrate binding.
<StructureSection load='1ebg' size='340' side='right'caption='[[1ebg]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ebg]] is a 2 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=1EBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EBG 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PAH:PHOSPHONOACETOHYDROXAMIC+ACID'>PAH</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=1ebg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ebg OCA], [https://pdbe.org/1ebg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ebg RCSB], [https://www.ebi.ac.uk/pdbsum/1ebg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ebg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ENO1_YEAST ENO1_YEAST]
== 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/eb/1ebg_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=1ebg ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1EBG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MG and PAH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EBG OCA].
*[[Enolase 3D structures|Enolase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Chelation of serine 39 to Mg2+ latches a gate at the active site of enolase: structure of the bis(Mg2+) complex of yeast enolase and the intermediate analog phosphonoacetohydroxamate at 2.1-A resolution., Wedekind JE, Poyner RR, Reed GH, Rayment I, Biochemistry. 1994 Aug 9;33(31):9333-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8049235 8049235]
[[Category: Large Structures]]
[[Category: Phosphopyruvate hydratase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Rayment I]]
[[Category: Rayment, I.]]
[[Category: Reed GH]]
[[Category: Reed, G.H.]]
[[Category: Wedekind JE]]
[[Category: Wedekind, J.E.]]
[[Category: MG]]
[[Category: PAH]]
[[Category: carbon-oxygen lyase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:52:34 2007''

Latest revision as of 07:00, 7 February 2024

CHELATION OF SER 39 TO MG2+ LATCHES A GATE AT THE ACTIVE SITE OF ENOLASE: STRUCTURE OF THE BIS(MG2+) COMPLEX OF YEAST ENOLASE AND THE INTERMEDIATE ANALOG PHOSPHONOACETOHYDROXAMATE AT 2.1 ANGSTROMS RESOLUTION

1ebg, resolution 2.10Å

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