1ju2

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[[Image:1ju2.jpg|left|200px]]<br /><applet load="1ju2" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ju2.jpg|left|200px]]
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caption="1ju2, resolution 1.47&Aring;" />
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'''Crystal structure of the hydroxynitrile lyase from almond'''<br />
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{{Structure
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|PDB= 1ju2 |SIZE=350|CAPTION= <scene name='initialview01'>1ju2</scene>, resolution 1.47&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=IPA:ISOPROPYL ALCOHOL'>IPA</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Mandelonitrile_lyase Mandelonitrile lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.10 4.1.2.10]
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|GENE=
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}}
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'''Crystal structure of the hydroxynitrile lyase from almond'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1JU2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Prunus_dulcis Prunus dulcis] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=IPA:'>IPA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Mandelonitrile_lyase Mandelonitrile lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.10 4.1.2.10] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JU2 OCA].
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1JU2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Prunus_dulcis Prunus dulcis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JU2 OCA].
==Reference==
==Reference==
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The hydroxynitrile lyase from almond: a lyase that looks like an oxidoreductase., Dreveny I, Gruber K, Glieder A, Thompson A, Kratky C, Structure. 2001 Sep;9(9):803-15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11566130 11566130]
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The hydroxynitrile lyase from almond: a lyase that looks like an oxidoreductase., Dreveny I, Gruber K, Glieder A, Thompson A, Kratky C, Structure. 2001 Sep;9(9):803-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11566130 11566130]
[[Category: Mandelonitrile lyase]]
[[Category: Mandelonitrile lyase]]
[[Category: Prunus dulcis]]
[[Category: Prunus dulcis]]
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[[Category: hydroxynitrile lyase]]
[[Category: hydroxynitrile lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:26:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:08:28 2008''

Revision as of 10:08, 20 March 2008

Image:1ju2.jpg


PDB ID 1ju2

Drag the structure with the mouse to rotate
, resolution 1.47Å
Ligands: , and
Activity: Mandelonitrile lyase, with EC number 4.1.2.10
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the hydroxynitrile lyase from almond


Overview

BACKGROUND: Cyanogenesis is a defense process of several thousand plant species. Hydroxynitrile lyase, a key enzyme of this process, cleaves a cyanohydrin into hydrocyanic acid and the corresponding aldehyde or ketone. The reverse reaction constitutes an important tool in biocatalysis. Different classes of hydroxynitrile lyases have convergently evolved from FAD-dependent oxidoreductases, alpha/beta hydrolases, and alcohol dehydrogenases. The FAD-dependent hydroxynitrile lyases (FAD-HNLs) carry a flavin cofactor whose redox properties appear to be unimportant for catalysis. RESULTS: We have determined the crystal structure of a 61 kDa hydroxynitrile lyase isoenzyme from Prunus amygdalus (PaHNL1) to 1.5 A resolution. Clear electron density originating from four glycosylation sites could be observed. As concerns the overall protein fold including the FAD cofactor, PaHNL1 belongs to the family of GMC oxidoreductases. The active site for the HNL reaction is probably at a very similar position as the active sites in homologous oxidases. CONCLUSIONS: There is strong evidence from the structure and the reaction product that FAD-dependent hydroxynitrile lyases have evolved from an aryl alcohol oxidizing precursor. Since key residues implicated in oxidoreductase activity are also present in PaHNL1, it is not obvious why this enzyme shows no oxidase activity. Similarly, features proposed to be relevant for hydroxy-nitrile lyase activity in other hydroxynitrile lyases, i.e., a general base and a positive charge to stabilize the cyanide, are not obviously present in the putative active site of PaHNL1. Therefore, the reason for its HNL activity is far from being well understood at this point.

About this Structure

1JU2 is a Single protein structure of sequence from Prunus dulcis. Full crystallographic information is available from OCA.

Reference

The hydroxynitrile lyase from almond: a lyase that looks like an oxidoreductase., Dreveny I, Gruber K, Glieder A, Thompson A, Kratky C, Structure. 2001 Sep;9(9):803-15. PMID:11566130

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