1e8d

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[[Image:1e8d.gif|left|200px]]<br /><applet load="1e8d" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1e8d.gif|left|200px]]
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caption="1e8d, resolution 2.20&Aring;" />
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'''MECHANISTIC ASPECTS OF CYANOGENESIS FROM ACTIVE SITE MUTANT SER80ALA OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA IN COMPLEX WITH ACETONE CYANOHYDRIN'''<br />
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{{Structure
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|PDB= 1e8d |SIZE=350|CAPTION= <scene name='initialview01'>1e8d</scene>, resolution 2.20&Aring;
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|SITE= <scene name='pdbsite=ASA:Active+Site+A.+Catalytic+Residue+SER+80+Is+Mutated+To+ALA'>ASA</scene> and <scene name='pdbsite=ASB:Active+Site+B.+Catalytic+Residue+SER+80+Is+Mutated+To+ALA'>ASB</scene>
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|LIGAND= <scene name='pdbligand=CNH:2-HYDROXY-2-METHYLPROPANENITRILE'>CNH</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_3.3.2.4 Transferred entry: 3.3.2.4], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.37 4.2.1.37]
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|GENE=
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}}
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'''MECHANISTIC ASPECTS OF CYANOGENESIS FROM ACTIVE SITE MUTANT SER80ALA OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA IN COMPLEX WITH ACETONE CYANOHYDRIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1E8D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Manihot_esculenta Manihot esculenta] with <scene name='pdbligand=CNH:'>CNH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_3.3.2.4 Transferred entry: 3.3.2.4], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.37 4.2.1.37] Known structural/functional Sites: <scene name='pdbsite=ASA:Active+Site+A.+Catalytic+Residue+SER+80+Is+Mutated+To+ALA'>ASA</scene> and <scene name='pdbsite=ASB:Active+Site+B.+Catalytic+Residue+SER+80+Is+Mutated+To+ALA'>ASB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8D OCA].
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1E8D 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=1E8D OCA].
==Reference==
==Reference==
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Mechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of hydroxynitrile lyase from Manihot esculenta in complex with acetone cyanohydrin., Lauble H, Miehlich B, Forster S, Wajant H, Effenberger F, Protein Sci. 2001 May;10(5):1015-22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11316882 11316882]
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Mechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of hydroxynitrile lyase from Manihot esculenta in complex with acetone cyanohydrin., Lauble H, Miehlich B, Forster S, Wajant H, Effenberger F, Protein Sci. 2001 May;10(5):1015-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11316882 11316882]
[[Category: Manihot esculenta]]
[[Category: Manihot esculenta]]
[[Category: Single protein]]
[[Category: Single protein]]
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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 12:25:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:51:33 2008''

Revision as of 08:51, 20 March 2008


PDB ID 1e8d

Drag the structure with the mouse to rotate
, resolution 2.20Å
Sites: and
Ligands:
Activity: Transferred entry: 3.3.2.4, with EC number 4.2.1.37
Coordinates: save as pdb, mmCIF, xml



MECHANISTIC ASPECTS OF CYANOGENESIS FROM ACTIVE SITE MUTANT SER80ALA OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA IN COMPLEX WITH ACETONE CYANOHYDRIN


Overview

The structure and function of hydroxynitrile lyase from Manihot esculenta (MeHNL) have been analyzed by X-ray crystallography and site-directed mutagenesis. The crystal structure of the MeHNL-S80A mutant enzyme has been refined to an R-factor of 18.0% against diffraction data to 2.1-A resolution. The three-dimensional structure of the MeHNL-S80A-acetone cyanohydrin complex was determined at 2.2-A resolution and refined to an R-factor of 18.7%. Thr11 and Cys81 involved in substrate binding have been substituted by Ala in site-directed mutagenesis. The kinetic measurements of these mutant enzymes are presented. Combined with structural data, the results support a mechanism for cyanogenesis in which His236 as a general base abstracts a proton from Ser80, thereby allowing proton transfer from the hydroxyl group of acetone cyanohydrin to Ser80. The His236 imidazolium cation then facilitates the leaving of the nitrile group by proton donating.

About this Structure

1E8D is a Single protein structure of sequence from Manihot esculenta. Full crystallographic information is available from OCA.

Reference

Mechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of hydroxynitrile lyase from Manihot esculenta in complex with acetone cyanohydrin., Lauble H, Miehlich B, Forster S, Wajant H, Effenberger F, Protein Sci. 2001 May;10(5):1015-22. PMID:11316882

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