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[[Image:1dwp.jpg|left|200px]]<br /><applet load="1dwp" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1dwp, resolution 2.2&Aring;" />
'''CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA AT 2.2 ANGSTROM RESOLUTION'''<br />


==About this Structure==
==Crystal Structure of Hydroxynitrile Lyase from Manihot esculenta at 2.2 Angstrom Resolution==
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 <scene name='pdbligand=ACT:'>ACT</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1DWP OCA].  
<StructureSection load='1dwp' size='340' side='right'caption='[[1dwp]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dw/1dwp_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1dwp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Manihot esculenta]]
[[Category: Manihot esculenta]]
[[Category: Single protein]]
[[Category: Effenberger F]]
[[Category: Transferred entry: 3.3.2.4]]
[[Category: Forster S]]
[[Category: Effenberger, F.]]
[[Category: Kratky C]]
[[Category: Forster, S.]]
[[Category: Lauble H]]
[[Category: Kratky, C.]]
[[Category: Mielich B]]
[[Category: Lauble, H.]]
[[Category: Wagner U]]
[[Category: Mielich, B.]]
[[Category: Wajant H]]
[[Category: Wagner, U.]]
[[Category: Wajant, H.]]
[[Category: ACT]]
[[Category: cyanogenesis]]
[[Category: hydroxynitrile lyase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:35:51 2008''
Retrieved from "https://proteopedia.org/1dwp"