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[[Image:1dwq.gif|left|200px]]<br />
<applet load="1dwq" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1dwq, resolution 2.2&Aring;" />
'''CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA IN COMPLEX WITH SUBSTRATES ACETONE AND CHLOROACETONE:IMPLICATIONS FOR THE MECHANISM OF CYANOGENESIS'''<br />


==Overview==
==Crystal Structure of Hydroxynitrile Lyase from Manihot esculenta in Complex with Substrates Acetone and Chloroacetone:Implications for the Mechanism of Cyanogenesis==
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.
<StructureSection load='1dwq' size='340' side='right'caption='[[1dwq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1dwq]] 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=1DWQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DWQ 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=ATO:CHLOROACETONE'>ATO</scene>, <scene name='pdbligand=CSA:S-ACETONYLCYSTEINE'>CSA</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=1dwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dwq OCA], [https://pdbe.org/1dwq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dwq RCSB], [https://www.ebi.ac.uk/pdbsum/1dwq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dwq 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/1dwq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1dwq 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.


==About this Structure==
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>
1DWQ 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 ATO 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]]. Structure known Active Sites: ASA and ASB. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DWQ OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11173464 11173464]
</div>
<div class="pdbe-citations 1dwq" 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: Lauble H]]
[[Category: Forster, S.]]
[[Category: Mielich B]]
[[Category: Lauble, H.]]
[[Category: Wajant H]]
[[Category: Mielich, B.]]
[[Category: Wajant, H.]]
[[Category: ATO]]
[[Category: chloroacetone complex]]
[[Category: hydroxynitrile lyase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:39:49 2007''

Latest revision as of 08:17, 9 April 2025

Crystal Structure of Hydroxynitrile Lyase from Manihot esculenta in Complex with Substrates Acetone and Chloroacetone:Implications for the Mechanism of Cyanogenesis

1dwq, resolution 2.20Å

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