1dwq
From Proteopedia
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|PDB= 1dwq |SIZE=350|CAPTION= <scene name='initialview01'>1dwq</scene>, resolution 2.2Å | |PDB= 1dwq |SIZE=350|CAPTION= <scene name='initialview01'>1dwq</scene>, resolution 2.2Å | ||
|SITE= <scene name='pdbsite=ASA:Catalytic+Triad+Active+Site'>ASA</scene> and <scene name='pdbsite=ASB:Catalytic+Triad+Active+Site'>ASB</scene> | |SITE= <scene name='pdbsite=ASA:Catalytic+Triad+Active+Site'>ASA</scene> and <scene name='pdbsite=ASB:Catalytic+Triad+Active+Site'>ASB</scene> | ||
| - | |LIGAND= <scene name='pdbligand=ATO:CHLOROACETONE'>ATO</scene> | + | |LIGAND= <scene name='pdbligand=ATO:CHLOROACETONE'>ATO</scene>, <scene name='pdbligand=CSA:S-ACETONYLCYSTEINE'>CSA</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=1dwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dwq OCA], [http://www.ebi.ac.uk/pdbsum/1dwq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dwq 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: Forster, S.]] | [[Category: Forster, S.]] | ||
| Line 28: | Line 31: | ||
[[Category: Mielich, B.]] | [[Category: Mielich, B.]] | ||
[[Category: Wajant, H.]] | [[Category: Wajant, H.]] | ||
| - | [[Category: ATO]] | ||
[[Category: chloroacetone complex]] | [[Category: chloroacetone complex]] | ||
[[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 19:50:18 2008'' |
Revision as of 16:50, 30 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| 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 | ||||||
CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA IN COMPLEX WITH SUBSTRATES ACETONE AND CHLOROACETONE:IMPLICATIONS FOR THE MECHANISM OF CYANOGENESIS
Overview
The crystal structures of hydroxynitrile lyase from Manihot esculenta (MeHNL) complexed with the native substrate acetone and substrate analogue chloroacetone have been determined and refined at 2.2 A resolution. The substrates are positioned in the active site by hydrogen-bond interactions of the carbonyl O atom with Thr11 OG, Ser80 OG and, to a lesser extent, Cys81 SG. These studies support a mechanism for cyanogenesis as well as for the stereospecific MeHNL-catalyzed formation of (S)-cyanohydrins, which closely resembles the base-catalyzed chemical reaction of HCN with carbonyl compounds.
About this Structure
1DWQ is a Single protein structure of sequence from Manihot esculenta. Full crystallographic information is available from OCA.
Reference
Structure of hydroxynitrile lyase from Manihot esculenta in complex with substrates acetone and chloroacetone: implications for the mechanism of cyanogenesis., Lauble H, Forster S, Miehlich B, Wajant H, Effenberger F, Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):194-200. PMID:11173464
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