1dwp

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[[Image:1dwp.jpg|left|200px]]<br /><applet load="1dwp" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dwp, resolution 2.2&Aring;" />
 
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'''CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA AT 2.2 ANGSTROM RESOLUTION'''<br />
 
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==About this Structure==
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==Crystal Structure of Hydroxynitrile Lyase from Manihot esculenta at 2.2 Angstrom Resolution==
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1DWP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Manihot_esculenta Manihot esculenta] with ACT as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_3.3.2.4 Transferred entry: 3.3.2.4], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.37 4.2.1.37] Known structural/functional Sites: <scene name='pdbsite=ASA:Catalytic Triad Active Site'>ASA</scene> and <scene name='pdbsite=ASB:Catalytic Triad Active Site'>ASB</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DWP OCA].
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<StructureSection load='1dwp' size='340' side='right'caption='[[1dwp]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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[[Category: Manihot esculenta]]
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== Structural highlights ==
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[[Category: Single protein]]
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<table><tr><td colspan='2'>[[1dwp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Manihot_esculenta Manihot esculenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DWP FirstGlance]. <br>
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[[Category: Transferred entry: 3.3.2.4]]
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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]] 2.2&#8491;</td></tr>
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[[Category: Effenberger, F.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
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[[Category: Forster, S.]]
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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=1dwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dwp OCA], [https://pdbe.org/1dwp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dwp RCSB], [https://www.ebi.ac.uk/pdbsum/1dwp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dwp ProSAT]</span></td></tr>
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[[Category: Kratky, C.]]
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</table>
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[[Category: Lauble, H.]]
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== Function ==
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[[Category: Mielich, B.]]
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[https://www.uniprot.org/uniprot/HNL_MANES HNL_MANES] Involved in cyanogenesis, the release of HCN from injured tissues. Decomposes a varieties of (R) or (S) cyanohydrins into HCN and the corresponding aldehydes and ketones. The natural substrate of this enzyme is (S)-acetone cyanohydrin.
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[[Category: Wagner, U.]]
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== Evolutionary Conservation ==
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[[Category: Wajant, H.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: ACT]]
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Check<jmol>
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[[Category: cyanogenesis]]
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<jmolCheckbox>
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[[Category: hydroxynitrile lyase]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dw/1dwp_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=1dwp 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 crystal structures of hydroxynitrile lyase from Manihot esculenta (MeHNL) complexed with the native substrate acetone and substrate analogue chloroacetone have been determined and refined at 2.2 A resolution. The substrates are positioned in the active site by hydrogen-bond interactions of the carbonyl O atom with Thr11 OG, Ser80 OG and, to a lesser extent, Cys81 SG. These studies support a mechanism for cyanogenesis as well as for the stereospecific MeHNL-catalyzed formation of (S)-cyanohydrins, which closely resembles the base-catalyzed chemical reaction of HCN with carbonyl compounds.
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:46:26 2007''
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Structure of hydroxynitrile lyase from Manihot esculenta in complex with substrates acetone and chloroacetone: implications for the mechanism of cyanogenesis.,Lauble H, Forster S, Miehlich B, Wajant H, Effenberger F Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):194-200. PMID:11173464<ref>PMID:11173464</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 1dwp" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Manihot esculenta]]
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[[Category: Effenberger F]]
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[[Category: Forster S]]
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[[Category: Kratky C]]
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[[Category: Lauble H]]
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[[Category: Mielich B]]
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[[Category: Wagner U]]
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[[Category: Wajant H]]

Current revision

Crystal Structure of Hydroxynitrile Lyase from Manihot esculenta at 2.2 Angstrom Resolution

PDB ID 1dwp

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