1eb9

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[[Image:1eb9.png|left|200px]]
 
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==Structure Determinants of Substrate Specificity of Hydroxynitrile Lyase from Manihot esculenta==
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The line below this paragraph, containing "STRUCTURE_1eb9", creates the "Structure Box" on the page.
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<StructureSection load='1eb9' size='340' side='right'caption='[[1eb9]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1eb9]] 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=1EB9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EB9 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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=HBA:P-HYDROXYBENZALDEHYDE'>HBA</scene></td></tr>
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{{STRUCTURE_1eb9| PDB=1eb9 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eb9 OCA], [https://pdbe.org/1eb9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eb9 RCSB], [https://www.ebi.ac.uk/pdbsum/1eb9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eb9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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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/eb/1eb9_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/main_output.php?pdb_ID=1eb9 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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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.
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===STRUCTURE DETERMINANTS OF SUBSTRATE SPECIFICITY OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA===
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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>
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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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The line below this paragraph, {{ABSTRACT_PUBMED_11742123}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1eb9" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11742123 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11742123}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[1eb9]] 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=1EB9 OCA].
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==Reference==
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<ref group="xtra">PMID:11742123</ref><ref group="xtra">PMID:11173464</ref><references group="xtra"/>
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[[Category: Manihot esculenta]]
[[Category: Manihot esculenta]]
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[[Category: Trans-epoxysuccinate hydrolase]]
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[[Category: Effenberger F]]
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[[Category: Effenberger, F.]]
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[[Category: Foerster S]]
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[[Category: Foerster, S.]]
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[[Category: Kobler C]]
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[[Category: Kobler, C.]]
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[[Category: Lauble H]]
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[[Category: Lauble, H.]]
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[[Category: Miehlich B]]
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[[Category: Miehlich, B.]]
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[[Category: Wajant H]]
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[[Category: Wajant, H.]]
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[[Category: Active-site tunnel mutant]]
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[[Category: Hydroxynitrile lyase]]
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[[Category: Lyase]]
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[[Category: Substrate specificity]]
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Current revision

Structure Determinants of Substrate Specificity of Hydroxynitrile Lyase from Manihot esculenta

PDB ID 1eb9

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