5eb5
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The crystal structure of almond HNL, PaHNL5 V317A, in complex with benzyl alcohol== |
| + | <StructureSection load='5eb5' size='340' side='right' caption='[[5eb5]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5eb5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EB5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EB5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=010:PHENYLMETHANOL'>010</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5eb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eb5 OCA], [http://pdbe.org/5eb5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eb5 RCSB], [http://www.ebi.ac.uk/pdbsum/5eb5 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Hydroxynitrile lyases (HNLs) catalyze the asymmetric addition of HCN to aldehydes producing enantiomerically pure cyanohydrins. These enzymes can be heterologously expressed in large quantities making them interesting candidates for industrial applications. The HNLs from Rosaceae evolved from flavin dependent dehydrogenase/oxidase structures. Here we report the high resolution X-ray structure of the highly glycosylated Prunus amygdalus HNL isoenzyme5 (PaHNL5 V317A) expressed in Aspergillus niger and its complex with benzyl alcohol. A comparison with the structure of isoenzyme PaHNL1 indicates a higher accessibility to the active site and a larger cavity for PaHNL5. Additionally, the PaHNL5 complex structure with benzyl alcohol was compared with the structurally related aryl-alcohol oxidase (AAO). Even though both enzymes contain an FAD-cofactor and histidine residues at crucial positions in the active site, PaHNL5 lacks the oxidoreductase activity. The structures indicate that in PaHNLs benzyl alcohol is bound too far away from the FAD cofactor in order to be oxidized. | ||
| - | + | Structures of almond hydroxynitrile lyase isoenzyme 5 provide a rationale for the lack of oxidoreductase activity in flavin dependent HNLs.,Pavkov-Keller T, Bakhuis J, Steinkellner G, Jolink F, Keijmel E, Birner-Gruenberger R, Gruber K J Biotechnol. 2016 Apr 8. pii: S0168-1656(16)30193-6. doi:, 10.1016/j.jbiotec.2016.04.013. PMID:27067080<ref>PMID:27067080</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5eb5" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Gruber, K]] | [[Category: Gruber, K]] | ||
| + | [[Category: Pavkov-Keller, T]] | ||
| + | [[Category: Steinkellner, G]] | ||
| + | [[Category: Benzyl alcohol]] | ||
| + | [[Category: Hydroxynitrile lyase]] | ||
| + | [[Category: Lyase]] | ||
| + | [[Category: Pahnl5]] | ||
Revision as of 19:23, 10 May 2016
The crystal structure of almond HNL, PaHNL5 V317A, in complex with benzyl alcohol
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