1gtz

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[[Image:1gtz.gif|left|200px]]
 
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{{Structure
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==Structure of STREPTOMYCES COELICOLOR TYPE II DEHYDROQUINASE R23A MUTANT IN COMPLEX WITH DEHYDROSHIKIMATE==
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|PDB= 1gtz |SIZE=350|CAPTION= <scene name='initialview01'>1gtz</scene>, resolution 1.6&Aring;
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<StructureSection load='1gtz' size='340' side='right'caption='[[1gtz]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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|SITE= <scene name='pdbsite=DHA:Dhk+Binding+Site+For+Chain+L'>DHA</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=DHK:3-DEHYDROSHIKIMATE'>DHK</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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<table><tr><td colspan='2'>[[1gtz]] 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=1GTZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GTZ FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/3-dehydroquinate_dehydratase 3-dehydroquinate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.10 4.2.1.10] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DHK:3-DEHYDROSHIKIMATE'>DHK</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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|DOMAIN=
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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=1gtz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gtz OCA], [https://pdbe.org/1gtz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gtz RCSB], [https://www.ebi.ac.uk/pdbsum/1gtz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gtz ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gtz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gtz OCA], [http://www.ebi.ac.uk/pdbsum/1gtz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gtz RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/AROQ_STRCO AROQ_STRCO] Catalyzes a trans-dehydration via an enolate intermediate (By similarity).[HAMAP-Rule:MF_00169]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gt/1gtz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1gtz ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''STRUCTURE OF STREPTOMYCES COELICOLOR TYPE II DEHYDROQUINASE R23A MUTANT IN COMPLEX WITH DEHYDROSHIKIMATE'''
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1gtz" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Dehydroquinase 3D structures|Dehydroquinase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1GTZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GTZ OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11937054 11937054]
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[[Category: 3-dehydroquinate dehydratase]]
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[[Category: Single protein]]
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[[Category: Streptomyces coelicolor]]
[[Category: Streptomyces coelicolor]]
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[[Category: Coggins, J R.]]
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[[Category: Coggins JR]]
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[[Category: Hunter, I S.]]
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[[Category: Hunter IS]]
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[[Category: Krell, T.]]
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[[Category: Krell T]]
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[[Category: Lapthorn, A J.]]
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[[Category: Lapthorn AJ]]
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[[Category: Robinson, D.]]
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[[Category: Robinson DA]]
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[[Category: Roszak, A W.]]
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[[Category: Roszak AW]]
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[[Category: dodecameric quaternary structure]]
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[[Category: lyase]]
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[[Category: shikimate pathway]]
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[[Category: tetrahedral symmetry aromatic amino acid biosynthesis]]
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[[Category: type ii dehydroquinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:51:14 2008''
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Current revision

Structure of STREPTOMYCES COELICOLOR TYPE II DEHYDROQUINASE R23A MUTANT IN COMPLEX WITH DEHYDROSHIKIMATE

PDB ID 1gtz

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