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| | <StructureSection load='1iyx' size='340' side='right'caption='[[1iyx]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='1iyx' size='340' side='right'caption='[[1iyx]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1iyx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterococcus_hirae Enterococcus hirae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IYX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1iyx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_hirae Enterococcus hirae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IYX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.8Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iyx OCA], [http://pdbe.org/1iyx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iyx RCSB], [http://www.ebi.ac.uk/pdbsum/1iyx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iyx 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=1iyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iyx OCA], [https://pdbe.org/1iyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iyx RCSB], [https://www.ebi.ac.uk/pdbsum/1iyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iyx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ENO_ENTHR ENO_ENTHR] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Enterococcus hirae]] | | [[Category: Enterococcus hirae]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphopyruvate hydratase]]
| + | [[Category: Hosaka T]] |
| - | [[Category: Hosaka, T]] | + | [[Category: Meguro T]] |
| - | [[Category: Meguro, T]] | + | [[Category: Shirakihara Y]] |
| - | [[Category: Shirakihara, Y]] | + | [[Category: Yamato I]] |
| - | [[Category: Yamato, I]] | + | |
| - | [[Category: Enolase family]]
| + | |
| - | [[Category: Lyase]]
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| Structural highlights
Function
ENO_ENTHR
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
We report the crystal structure of an enolase from Enterococcus hirae, which is the first report of a structure determination among gram-positive bacteria. We isolated the enolase gene and determined the base sequence. The amino acid sequence deduced from the DNA sequence suggests that this enolase is composed of 431 amino acids. The amino acid sequence is very similar to those of enolases from eukaryotic and prokaryotic organisms, being 65% and 50% identical to enolases from Escherichia coli and yeast, respectively. The enolase prepared from E. hirae lysate yielded crystals containing one dimer per asymmetric unit. X-ray diffraction patterns were obtained at 2.8 A resolution on a SPring-8 synchrotron radiation source. Crystals belong to space group I4 with unit cell dimensions of a = b = 153.5 A, c = 90.7 A. The E. hirae, yeast, E. coli and lobster enolase structures are very similar. The E. hirae enolase takes an "Open" conformation. The regions in the structure that differ most from other enolases are loops L4 (132-140) and L3 (244-265). Considering the positions of these loops relative to the active site, they seem to have no direct involvement in function. Our findings show that the three dimensional structure of an important enzyme in the glycolytic pathway is evolutionarily conserved among eukaryotes and prokaryotes, including gram-positive bacteria.
Crystal structure of Enterococcus hirae enolase at 2.8 A resolution.,Hosaka T, Meguro T, Yamato I, Shirakihara Y J Biochem. 2003 Jun;133(6):817-23. PMID:12869539[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hosaka T, Meguro T, Yamato I, Shirakihara Y. Crystal structure of Enterococcus hirae enolase at 2.8 A resolution. J Biochem. 2003 Jun;133(6):817-23. PMID:12869539
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