2gpt

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[[Image:2gpt.gif|left|200px]]
 
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{{Structure
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==Crystal structure of Arabidopsis Dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate==
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|PDB= 2gpt |SIZE=350|CAPTION= <scene name='initialview01'>2gpt</scene>, resolution 1.95&Aring;
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<StructureSection load='2gpt' size='340' side='right'caption='[[2gpt]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SKM:(3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC+ACID'>SKM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>
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<table><tr><td colspan='2'>[[2gpt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GPT FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.95&#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=SKM:(3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC+ACID'>SKM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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=2gpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gpt OCA], [https://pdbe.org/2gpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gpt RCSB], [https://www.ebi.ac.uk/pdbsum/2gpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gpt 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=2gpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gpt OCA], [http://www.ebi.ac.uk/pdbsum/2gpt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gpt RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/DHQSD_ARATH DHQSD_ARATH]
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== Evolutionary Conservation ==
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'''Crystal structure of Arabidopsis Dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gp/2gpt_consurf.spt"</scriptWhenChecked>
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The bifunctional enzyme dehydroquinate dehydratase-shikimate dehydrogenase (DHQ-SDH) catalyzes the dehydration of dehydroquinate to dehydroshikimate and the reduction of dehydroshikimate to shikimate in the shikimate pathway. We report the first crystal structure of Arabidopsis DHQ-SDH with shikimate bound at the SDH site and tartrate at the DHQ site. The interactions observed in the DHQ-tartrate complex reveal a conserved mode for substrate binding between the plant and microbial DHQ dehydratase family of enzymes. The SDH-shikimate complex provides the first direct evidence of the role of active site residues in the catalytic mechanism. Site-directed mutagenesis and mechanistic analysis revealed that Asp 423 and Lys 385 are key catalytic groups and Ser 336 is a key binding group. The arrangement of the two functional domains reveals that the control of metabolic flux through the shikimate pathway is achieved by increasing the effective concentration of dehydroshikimate through the proximity of the two sites.
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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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==About this Structure==
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</jmolCheckbox>
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2GPT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GPT OCA].
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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=2gpt ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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Structure of Arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase and implications for metabolic channeling in the shikimate pathway., Singh SA, Christendat D, Biochemistry. 2006 Jun 27;45(25):7787-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16784230 16784230]
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</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Christendat, D.]]
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[[Category: Christendat D]]
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[[Category: Singh, S A.]]
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[[Category: Singh SA]]
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[[Category: arabidopsis thaliana]]
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[[Category: aroe]]
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[[Category: bifunctional enzyme]]
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[[Category: shikimate]]
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[[Category: shikimate dehydrogenase]]
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[[Category: tartrate]]
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[[Category: type i dehydroquinate dehydratase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:19:51 2008''
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Current revision

Crystal structure of Arabidopsis Dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate

PDB ID 2gpt

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