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1ynu
From Proteopedia
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| - | [[Image:1ynu.gif|left|200px]] | + | [[Image:1ynu.gif|left|200px]] |
| - | + | ||
| - | '''Crystal structure of apple ACC synthase in complex with L-vinylglycine''' | + | {{Structure |
| + | |PDB= 1ynu |SIZE=350|CAPTION= <scene name='initialview01'>1ynu</scene>, resolution 2.25Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PY4:2-[O-PHOSPHONOPYRIDOXYL]-AMINO-+BUTYRIC+ACID'>PY4</scene> and <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/1-aminocyclopropane-1-carboxylate_synthase 1-aminocyclopropane-1-carboxylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.14 4.4.1.14] | ||
| + | |GENE= ACS-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3750 Malus x domestica]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of apple ACC synthase in complex with L-vinylglycine''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YNU is a [ | + | 1YNU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Malus_x_domestica Malus x domestica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YNU OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of ACC synthase inactivated by the mechanism-based inhibitor L-vinylglycine., Capitani G, Tschopp M, Eliot AC, Kirsch JF, Grutter MG, FEBS Lett. 2005 Apr 25;579(11):2458-62. PMID:[http:// | + | Structure of ACC synthase inactivated by the mechanism-based inhibitor L-vinylglycine., Capitani G, Tschopp M, Eliot AC, Kirsch JF, Grutter MG, FEBS Lett. 2005 Apr 25;579(11):2458-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15848188 15848188] |
[[Category: 1-aminocyclopropane-1-carboxylate synthase]] | [[Category: 1-aminocyclopropane-1-carboxylate synthase]] | ||
[[Category: Malus x domestica]] | [[Category: Malus x domestica]] | ||
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[[Category: lyase]] | [[Category: 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 15:25:15 2008'' |
Revision as of 13:25, 20 March 2008
| |||||||
| , resolution 2.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Gene: | ACS-1 (Malus x domestica) | ||||||
| Activity: | 1-aminocyclopropane-1-carboxylate synthase, with EC number 4.4.1.14 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of apple ACC synthase in complex with L-vinylglycine
Overview
L-Vinylglycine (L-VG) is both a substrate for and a mechanism-based inhibitor of 1-aminocyclopropane-1-carboxylate (ACC) synthase. The ratio of the rate constants for catalytic conversion to alpha-ketobutyrate and ammonia to inactivation is 500/1. The crystal structure of the covalent adduct of the inactivated enzyme was determined at 2.25 Angstroms resolution. The active site contains an external aldimine of the adduct of L-VG with the pyridoxal 5'-phosphate cofactor. The side chain gamma-carbon of L-VG is covalently bound to the epsilon-amino group of Lys273. This species corresponds to one of the two alternatives proposed by Feng and Kirsch [Feng, L. and Kirsch, J.F. (2000) L-Vinylglycine is an alternative substrate as well as a mechanism-based inhibitor of 1-aminocyclopropane-1-carboxylate synthase. Biochemistry 39, 2436-2444] and presumably results from Michael addition to a vinylglycine ketimine intermediate.
About this Structure
1YNU is a Single protein structure of sequence from Malus x domestica. Full crystallographic information is available from OCA.
Reference
Structure of ACC synthase inactivated by the mechanism-based inhibitor L-vinylglycine., Capitani G, Tschopp M, Eliot AC, Kirsch JF, Grutter MG, FEBS Lett. 2005 Apr 25;579(11):2458-62. PMID:15848188
Page seeded by OCA on Thu Mar 20 15:25:15 2008
