1yqd

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[[Image:1yqd.gif|left|200px]]
 
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==Sinapyl Alcohol Dehydrogenase complexed with NADP+==
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The line below this paragraph, containing "STRUCTURE_1yqd", creates the "Structure Box" on the page.
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<StructureSection load='1yqd' size='340' side='right'caption='[[1yqd]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1yqd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Populus_tremuloides Populus tremuloides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YQD FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.65&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1yqd| PDB=1yqd | SCENE= }}
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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=1yqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yqd OCA], [https://pdbe.org/1yqd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yqd RCSB], [https://www.ebi.ac.uk/pdbsum/1yqd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yqd ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q94G59_POPTM Q94G59_POPTM]
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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/yq/1yqd_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=1yqd ConSurf].
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<div style="clear:both"></div>
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'''Sinapyl Alcohol Dehydrogenase complexed with NADP+'''
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==See Also==
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*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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We describe the three-dimensional structure of sinapyl alcohol dehydrogenase (SAD) from Populus tremuloides (aspen), a member of the NADP(H)-dependent dehydrogenase family that catalyzes the last reductive step in the formation of monolignols. The active site topology revealed by the crystal structure substantiates kinetic results indicating that SAD maintains highest specificity for the substrate sinapaldehyde. We also report substantial substrate inhibition kinetics for the SAD-catalyzed reduction of hydroxycinnamaldehydes. Although SAD and classical cinnamyl alcohol dehydrogenases (CADs) catalyze the same reaction and share some sequence identity, the active site topology of SAD is strikingly different from that predicted for classical CADs. Kinetic analyses of wild-type SAD and several active site mutants demonstrate the complexity of defining determinants of substrate specificity in these enzymes. These results, along with a phylogenetic analysis, support the inclusion of SAD in a plant alcohol dehydrogenase subfamily that includes cinnamaldehyde and benzaldehyde dehydrogenases. We used the SAD three-dimensional structure to model several of these SAD-like enzymes, and although their active site topologies largely mirror that of SAD, we describe a correlation between substrate specificity and amino acid substitution patterns in their active sites. The SAD structure thus provides a framework for understanding substrate specificity in this family of enzymes and for engineering new enzyme specificities.
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[[Category: Large Structures]]
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==About this Structure==
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1YQD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Populus_tremuloides Populus tremuloides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQD OCA].
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==Reference==
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Structural and kinetic basis for substrate selectivity in Populus tremuloides sinapyl alcohol dehydrogenase., Bomati EK, Noel JP, Plant Cell. 2005 May;17(5):1598-611. Epub 2005 Apr 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15829607 15829607]
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[[Category: Cinnamyl-alcohol dehydrogenase]]
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[[Category: Populus tremuloides]]
[[Category: Populus tremuloides]]
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[[Category: Single protein]]
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[[Category: Bomati EK]]
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[[Category: Bomati, E K.]]
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[[Category: Noel JP]]
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[[Category: Noel, J P.]]
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[[Category: Biosynthesis]]
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[[Category: Lignin]]
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[[Category: Medium-chain dehydrogense/reductase]]
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[[Category: Monolignol]]
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[[Category: Oxidoreductase]]
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[[Category: Plant defense]]
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[[Category: Substrate inhibition]]
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[[Category: Zinc-dependent]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:38:49 2008''
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Current revision

Sinapyl Alcohol Dehydrogenase complexed with NADP+

PDB ID 1yqd

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