1m4n | pdb_00001m4n
CRYSTAL STRUCTURE OF APPLE ACC SYNTHASE IN COMPLEX WITH [2-(AMINO-OXY)ETHYL](5'-DEOXYADENOSIN-5'-YL)(METHYL)SULFONIUM
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| 1m4n, resolution 2.01Å | |||||||||||||
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| Ligands: | PLP, AAD and MES | ||||||||||||
| Activity: | 1-aminocyclopropane-1-carboxylate synthase, with EC number 4.4.1.14 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
The crystal structure of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with the substrate analogue [2-(amino-oxy)ethyl](5'-deoxyadenosin-5'-yl)(methyl)sulfonium (AMA) was determined at 2.01-A resolution. The crystallographic results show that a covalent adduct (oxime) is formed between AMA (an amino-oxy analogue of the natural substrate S-adenosyl-L-methionine (SAM)) and the pyridoxal 5'-phosphate (PLP) cofactor of ACC synthase. The oxime formation is supported by spectroscopic data. The ACC synthase-AMA structure provides reliable and detailed information on the binding mode of the natural substrate of ACC synthase and complements previous structural and functional work on this enzyme.
About this Structure
1M4N is a Single protein structure of sequence from Malus x domestica. Full crystallographic information is available from OCA.
Reference
Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding., Capitani G, Eliot AC, Gut H, Khomutov RM, Kirsch JF, Grutter MG, Biochim Biophys Acta. 2003 Apr 11;1647(1-2):55-60. PMID:12686108
Page seeded by OCA on Sun Mar 23 12:42:57 2008
