1els: Difference between revisions

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<StructureSection load='1els' size='340' side='right'caption='[[1els]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1els' size='340' side='right'caption='[[1els]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1els]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ELS FirstGlance]. <br>
<table><tr><td colspan='2'>[[1els]] is a 1 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=1ELS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ELS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PAH:PHOSPHONOACETOHYDROXAMIC+ACID'>PAH</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]] 2.4&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=1els FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1els OCA], [https://pdbe.org/1els PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1els RCSB], [https://www.ebi.ac.uk/pdbsum/1els PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1els 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=1els FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1els OCA], [https://pdbe.org/1els PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1els RCSB], [https://www.ebi.ac.uk/pdbsum/1els PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1els ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ENO1_YEAST ENO1_YEAST]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1els ConSurf].
</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=1els ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enolase, a glycolytic enzyme that catalyzes the dehydration of 2-phospho-D-glycerate (PGA) to form phosphoenolpyruvate (PEP), requires two divalent metal ions per active site for activity. The first metal ion, traditionally referred to as "conformational", binds in a high-affinity site I. The second metal ion, "catalytic", binds in site II only in the presence of a substrate or substrate analogue and with much lower affinity for the physiological cofactor Mg2+. While the high-affinity site has been well characterized, the position of the lower affinity site has not been established so far. Here, we report the structure of the quaternary complex between enolase, the transition-state analogue phosphonoacetohydroxamate (PhAH), and two Mn2+ ions. The structure has been refined by using 16 561 reflections with F/sigma (F) &gt; or = 3 to an R = 0.165 with average deviations of bond lengths and bond angles from ideal values of 0.013 A and 3.1 degrees, respectively. The "catalytic" metal ion is coordinated to two oxygen atoms of the phosphono moiety of PhAH and to the carbonyl oxygen of Gly37. Most likely, disordered water molecules complement its coordination sphere. The interaction with the site II metal ion must stabilize negative charge on the phosphate group and produce electron withdrawal from carbon 2 of the substrate, facilitating proton abstraction from carbon 2, the rate-limiting step in the catalytic process. The Gly37 residue is located in the flexible loop Ser36-His43, which assumes an "open" conformation in the absence of substrate and a "closed" conformation in the presence of a substrate.(ABSTRACT TRUNCATED AT 250 WORDS)
Catalytic metal ion binding in enolase: the crystal structure of an enolase-Mn2+-phosphonoacetohydroxamate complex at 2.4-A resolution.,Zhang E, Hatada M, Brewer JM, Lebioda L Biochemistry. 1994 May 24;33(20):6295-300. PMID:8193144<ref>PMID:8193144</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1els" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Enolase 3D structures|Enolase 3D structures]]
*[[Enolase 3D structures|Enolase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Phosphopyruvate hydratase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Brewer, J M]]
[[Category: Brewer JM]]
[[Category: Hatada, M]]
[[Category: Hatada M]]
[[Category: Lebioda, L]]
[[Category: Lebioda L]]
[[Category: Zhang, E]]
[[Category: Zhang E]]
[[Category: Carbon-oxygen lyase]]

Latest revision as of 10:04, 7 February 2024

CATALYTIC METAL ION BINDING IN ENOLASE: THE CRYSTAL STRUCTURE OF ENOLASE-MN2+-PHOSPHONOACETOHYDROXAMATE COMPLEX AT 2.4 ANGSTROMS RESOLUTIONCATALYTIC METAL ION BINDING IN ENOLASE: THE CRYSTAL STRUCTURE OF ENOLASE-MN2+-PHOSPHONOACETOHYDROXAMATE COMPLEX AT 2.4 ANGSTROMS RESOLUTION

Structural highlights

1els is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ENO1_YEAST

Evolutionary Conservation

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

See Also

1els, resolution 2.40Å

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