1eb8: Difference between revisions

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{{Seed}}
[[Image:1eb8.png|left|200px]]


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==Structure Determinants of Substrate Specificity of Hydroxynitrile Lyase from Manihot esculenta==
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<StructureSection load='1eb8' size='340' side='right'caption='[[1eb8]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1eb8]] 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=1EB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EB8 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
{{STRUCTURE_1eb8|  PDB=1eb8  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eb8 OCA], [https://pdbe.org/1eb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eb8 RCSB], [https://www.ebi.ac.uk/pdbsum/1eb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eb8 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/eb/1eb8_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=1eb8 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tryptophan 128 of hydroxynitrile lyase of Manihot esculenta (MeHNL) covers a significant part of a hydrophobic channel that gives access to the active site of the enzyme. This residue was therefore substituted in the mutant MeHNL-W128A by alanine to study its importance for the substrate specificity of the enzyme. Wild-type MeHNL and MeHNL-W128A showed comparable activity on the natural substrate acetone cyanohydrin (53 and 40 U/mg, respectively). However, the specific activities of MeHNL-W128A for the unnatural substrates mandelonitrile and 4-hydroxymandelonitrile are increased 9-fold and approximately 450-fold, respectively, compared with the wild-type MeHNL. The crystal structure of the MeHNL-W128A substrate-free form at 2.1 A resolution indicates that the W128A substitution has significantly enlarged the active-site channel entrance, and thereby explains the observed changes in substrate specificity for bulky substrates. Surprisingly, the MeHNL-W128A--4-hydroxybenzaldehyde complex structure at 2.1 A resolution shows the presence of two hydroxybenzaldehyde molecules in a sandwich type arrangement in the active site with an additional hydrogen bridge to the reacting center.


===STRUCTURE DETERMINANTS OF SUBSTRATE SPECIFICITY OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA===
Structure determinants of substrate specificity of hydroxynitrile lyase from Manihot esculenta.,Lauble H, Miehlich B, Forster S, Kobler C, Wajant H, Effenberger F Protein Sci. 2002 Jan;11(1):65-71. PMID:11742123<ref>PMID:11742123</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1eb8" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 11742123 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_11742123}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1EB8 is a [[Single protein]] structure of 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=1EB8 OCA].
 
==Reference==
Structure determinants of substrate specificity of hydroxynitrile lyase from Manihot esculenta., Lauble H, Miehlich B, Forster S, Kobler C, Wajant H, Effenberger F, Protein Sci. 2002 Jan;11(1):65-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11742123 11742123]
[[Category: Manihot esculenta]]
[[Category: Manihot esculenta]]
[[Category: Single protein]]
[[Category: Effenberger F]]
[[Category: Trans-epoxysuccinate hydrolase]]
[[Category: Foerster S]]
[[Category: Effenberger, F.]]
[[Category: Kobler C]]
[[Category: Foerster, S.]]
[[Category: Lauble H]]
[[Category: Kobler, C.]]
[[Category: Miehlich B]]
[[Category: Lauble, H.]]
[[Category: Wajant H]]
[[Category: Miehlich, B.]]
[[Category: Wajant, H.]]
[[Category: Active-site tunnel mutant]]
[[Category: Hydroxynitrile lyase]]
[[Category: Lyase]]
[[Category: Substrate specificity]]
 
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Retrieved from "https://proteopedia.org/1eb8"