1d0i
From Proteopedia
(Difference between revisions)
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<StructureSection load='1d0i' size='340' side='right'caption='[[1d0i]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1d0i' size='340' side='right'caption='[[1d0i]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1d0i]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D0I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D0I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1d0i]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D0I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D0I FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d0i OCA], [https://pdbe.org/1d0i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d0i RCSB], [https://www.ebi.ac.uk/pdbsum/1d0i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d0i 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=1d0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d0i OCA], [https://pdbe.org/1d0i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d0i RCSB], [https://www.ebi.ac.uk/pdbsum/1d0i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d0i ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/AROQ_STRCO AROQ_STRCO] Catalyzes a trans-dehydration via an enolate intermediate (By similarity).[HAMAP-Rule:MF_00169] | |
== 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=1d0i 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=1d0i ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The structure of the type II DHQase from Streptomyces coelicolor has been solved and refined to high resolution in complexes with a number of ligands, including dehydroshikimate and a rationally designed transition state analogue, 2,3-anhydro-quinic acid. These structures define the active site of the enzyme and the role of key amino acid residues and provide snap shots of the catalytic cycle. The resolution of the flexible lid domain (residues 21-31) shows that the invariant residues Arg23 and Tyr28 close over the active site cleft. The tyrosine acts as the base in the initial proton abstraction, and evidence is provided that the reaction proceeds via an enol intermediate. The active site of the structure of DHQase in complex with the transition state analog also includes molecules of tartrate and glycerol, which provide a basis for further inhibitor design. | ||
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| - | The structure and mechanism of the type II dehydroquinase from Streptomyces coelicolor.,Roszak AW, Robinson DA, Krell T, Hunter IS, Fredrickson M, Abell C, Coggins JR, Lapthorn AJ Structure. 2002 Apr;10(4):493-503. PMID:11937054<ref>PMID:11937054</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1d0i" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Dehydroquinase 3D structures|Dehydroquinase 3D structures]] | *[[Dehydroquinase 3D structures|Dehydroquinase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: 3-dehydroquinate dehydratase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Streptomyces coelicolor]] |
| - | [[Category: | + | [[Category: Coggins JR]] |
| - | [[Category: | + | [[Category: Hunter IS]] |
| - | [[Category: | + | [[Category: Krell T]] |
| - | [[Category: | + | [[Category: Lapthorn AJ]] |
| - | [[Category: | + | [[Category: Roszak AW]] |
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Current revision
CRYSTAL STRUCTURE OF TYPE II DEHYDROQUINASE FROM STREPTOMYCES COELICOLOR COMPLEXED WITH PHOSPHATE IONS
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