1ynu: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[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== | ||
| Line 7: | Line 16: | ||
==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]] | ||
| Line 25: | Line 34: | ||
[[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
| |||||||||||||
| 1ynu, resolution 2.25Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | NI, K, PY4 and TRS | ||||||||||||
| 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
