1e89

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[[Image:1e89.png|left|200px]]
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==ON THE MECHANISM OF CYANOGENESIS CATALYZED BY HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA. CRYSTAL STRUCTURE OF ACTIVE SITE MUTANT SER80ALA IN COMPLEX WITH ACETONE CYANOHYDRIN==
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<StructureSection load='1e89' size='340' side='right' caption='[[1e89]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1e89]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Manihot_esculenta Manihot esculenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E89 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E89 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dwo|1dwo]], [[1dwp|1dwp]], [[1dwq|1dwq]]</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-epoxysuccinate_hydrolase Trans-epoxysuccinate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.4 3.3.2.4] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e89 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e89 RCSB], [http://www.ebi.ac.uk/pdbsum/1e89 PDBsum]</span></td></tr>
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<table>
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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/e8/1e89_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/chain_selection.php?pdb_ID=2ata 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 and function of hydroxynitrile lyase from Manihot esculenta (MeHNL) have been analyzed by X-ray crystallography and site-directed mutagenesis. The crystal structure of the MeHNL-S80A mutant enzyme has been refined to an R-factor of 18.0% against diffraction data to 2.1-A resolution. The three-dimensional structure of the MeHNL-S80A-acetone cyanohydrin complex was determined at 2.2-A resolution and refined to an R-factor of 18.7%. Thr11 and Cys81 involved in substrate binding have been substituted by Ala in site-directed mutagenesis. The kinetic measurements of these mutant enzymes are presented. Combined with structural data, the results support a mechanism for cyanogenesis in which His236 as a general base abstracts a proton from Ser80, thereby allowing proton transfer from the hydroxyl group of acetone cyanohydrin to Ser80. The His236 imidazolium cation then facilitates the leaving of the nitrile group by proton donating.
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{{STRUCTURE_1e89| PDB=1e89 | SCENE= }}
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Mechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of hydroxynitrile lyase from Manihot esculenta in complex with acetone cyanohydrin.,Lauble H, Miehlich B, Forster S, Wajant H, Effenberger F Protein Sci. 2001 May;10(5):1015-22. PMID:11316882<ref>PMID:11316882</ref>
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===ON THE MECHANISM OF CYANOGENESIS CATALYZED BY HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA. CRYSTAL STRUCTURE OF ACTIVE SITE MUTANT SER80ALA IN COMPLEX WITH ACETONE CYANOHYDRIN===
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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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{{ABSTRACT_PUBMED_11316882}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1e89]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Manihot_esculenta Manihot esculenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E89 OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:011316882</ref><references group="xtra"/>
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[[Category: Manihot esculenta]]
[[Category: Manihot esculenta]]
[[Category: Trans-epoxysuccinate hydrolase]]
[[Category: Trans-epoxysuccinate hydrolase]]

Revision as of 15:30, 29 September 2014

ON THE MECHANISM OF CYANOGENESIS CATALYZED BY HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA. CRYSTAL STRUCTURE OF ACTIVE SITE MUTANT SER80ALA IN COMPLEX WITH ACETONE CYANOHYDRIN

1e89, resolution 2.10Å

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