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[[Image:3yas.jpg|left|200px]]<br /><applet load="3yas" size="350" color="white" frame="true" align="right" spinBox="true"
caption="3yas, resolution 1.85&Aring;" />
'''HYDROXYNITRILE LYASE COMPLEXED WITH ACETONE'''<br />


==Overview==
==HYDROXYNITRILE LYASE COMPLEXED WITH ACETONE==
The 3D structures of complexes between the hydroxynitrile lyase from Hevea brasiliensis (Hb-HNL) and several substrate and/or inhibitor molecules, including trichloracetaldehyde, hexafluoracetone, acetone, and rhodanide, were determined by X-ray crystallography. The complex with trichloracetaldehyde showed a covalent linkage between the protein and the inhibitor, which had apparently resulted from nucleophilic attack of the catalytic Ser80-Ogamma. All other complexes showed the substrate or inhibitor molecule merely hydrogen bonded to the protein. In addition, the native crystal structure of Hb-HNL was redetermined at cryo-temperature and at room temperature, eliminating previous uncertainties concerning residual electron density within the active site, and leading to the observation of two conserved water molecules. One of them was found to be conserved in all complex structures and appears to have mainly structural significance. The other water molecule is conserved in all structures except for the complex with rhodanide; it is hydrogen bonded to the imidazole of the catalytic His235 and appears to affect the Hb-HNL catalyzed reaction. The observed 3D structural data suggest implications for the enzyme mechanism. It appears that the enzyme-catalyzed cyanohydrin formation is unlikely to proceed via a hemiacetal or hemiketal intermediate covalently attached to the enzyme, despite the observation of such an intermediate for the complex with trichloracetaldehyde. Instead, the data are consistent with a mechanism where the incoming substrate is activated by hydrogen bonding with its carbonyl oxygen to the Ser80 and Thr11 hydroxy groups. A hydrogen cyanide molecule subsequently replaces a water molecule and is deprotonated presumably by the His235 base. Deprotonation is facilitated by the proximity of the positive charge of the Lys236 side chain.
<StructureSection load='3yas' size='340' side='right'caption='[[3yas]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[3yas]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hevea_brasiliensis Hevea brasiliensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3YAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3YAS FirstGlance]. <br>
3YAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hevea_brasiliensis Hevea brasiliensis] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ACN:'>ACN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transfered_to_EC_4.1.2.37 Transfered to EC 4.1.2.37], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.39 4.1.2.39] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3YAS OCA].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3yas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3yas OCA], [https://pdbe.org/3yas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3yas RCSB], [https://www.ebi.ac.uk/pdbsum/3yas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3yas ProSAT]</span></td></tr>
Three-dimensional structures of enzyme-substrate complexes of the hydroxynitrile lyase from Hevea brasiliensis., Zuegg J, Gruber K, Gugganig M, Wagner UG, Kratky C, Protein Sci. 1999 Oct;8(10):1990-2000. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10548044 10548044]
</table>
== Function ==
[https://www.uniprot.org/uniprot/HNL_HEVBR HNL_HEVBR] 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/ya/3yas_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=3yas ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Hevea brasiliensis]]
[[Category: Hevea brasiliensis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Transfered to EC 4 1.2 37]]
[[Category: Gugganig M]]
[[Category: Gugganig, M.]]
[[Category: Kratky C]]
[[Category: Kratky, C.]]
[[Category: Wagner UG]]
[[Category: Wagner, U G.]]
[[Category: Zuegg J]]
[[Category: Zuegg, J.]]
[[Category: ACN]]
[[Category: SO4]]
[[Category: cyanogenesis]]
[[Category: cyanohydrin formation]]
[[Category: lyase]]
[[Category: oxynitrilase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:11:50 2008''

Latest revision as of 14:28, 14 March 2024

HYDROXYNITRILE LYASE COMPLEXED WITH ACETONE

3yas, resolution 1.85Å

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