1e89
From Proteopedia
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| - | [[Image:1e89.gif|left|200px]] | + | [[Image:1e89.gif|left|200px]] |
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| - | '''ON THE MECHANISM OF CYANOGENESIS CATALYZED BY HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA. CRYSTAL STRUCTURE OF ACTIVE SITE MUTANT SER80ALA IN COMPLEX WITH ACETONE CYANOHYDRIN''' | + | {{Structure |
| + | |PDB= 1e89 |SIZE=350|CAPTION= <scene name='initialview01'>1e89</scene>, resolution 2.10Å | ||
| + | |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> | ||
| + | |LIGAND= | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ON THE MECHANISM OF CYANOGENESIS CATALYZED BY HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA. CRYSTAL STRUCTURE OF ACTIVE SITE MUTANT SER80ALA IN COMPLEX WITH ACETONE CYANOHYDRIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E89 is a [ | + | 1E89 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=1E89 OCA]. |
==Reference== | ==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:[http:// | + | 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]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:51:29 2008'' |
Revision as of 08:51, 20 March 2008
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| , resolution 2.10Å | |||||||
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| Sites: | and | ||||||
| Activity: | Transferred entry: 3.3.2.4, with EC number 4.2.1.37 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ON THE MECHANISM OF CYANOGENESIS CATALYZED BY HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA. CRYSTAL STRUCTURE OF ACTIVE SITE MUTANT SER80ALA 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
1E89 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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