1e8d
From Proteopedia
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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> | |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= <scene name='pdbligand=CNH:2-HYDROXY-2-METHYLPROPANENITRILE'>CNH</scene> | |LIGAND= <scene name='pdbligand=CNH:2-HYDROXY-2-METHYLPROPANENITRILE'>CNH</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/ | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-epoxysuccinate_hydrolase Trans-epoxysuccinate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.4 3.3.2.4] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8d OCA], [http://www.ebi.ac.uk/pdbsum/1e8d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e8d RCSB]</span> | ||
}} | }} | ||
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[[Category: Manihot esculenta]] | [[Category: Manihot esculenta]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: | + | [[Category: Trans-epoxysuccinate hydrolase]] |
[[Category: Effenberger, F.]] | [[Category: Effenberger, F.]] | ||
[[Category: Foerster, S.]] | [[Category: Foerster, S.]] | ||
| Line 28: | Line 31: | ||
[[Category: Miehlich, B.]] | [[Category: Miehlich, B.]] | ||
[[Category: Wajant, H.]] | [[Category: Wajant, H.]] | ||
| - | [[Category: CNH]] | ||
[[Category: acetone cyanohydrin complex]] | [[Category: acetone cyanohydrin complex]] | ||
[[Category: active site mutant]] | [[Category: active site mutant]] | ||
[[Category: hydroxynitrile lyase]] | [[Category: hydroxynitrile lyase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:57:18 2008'' |
Revision as of 16:57, 30 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | |||||||
| Activity: | Trans-epoxysuccinate hydrolase, with EC number 3.3.2.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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