1M4N

CRYSTAL STRUCTURE OF APPLE ACC SYNTHASE IN COMPLEX WITH [2-(AMINO-OXY)ETHYL](5'-DEOXYADENOSIN-5'-YL)(METHYL)SULFONIUM

Summary for 1M4N

• Entry DOI: 10.2210/pdb1m4n/pdb
• Related: 1b8g
• Descriptor: 1-aminocyclopropane-1-carboxylate synthase, PYRIDOXAL-5'-PHOSPHATE, (2-AMINOOXY-ETHYL)-[5-(6-AMINO-PURIN-9-YL)-3,4-DIHYDROXY-TETRAHYDRO-FURAN-2-YLMETHYL]-METHYL-SULFONIUM, ... (5 entities in total)
• Functional Keywords: fruit ripening, ethylene biosynthesis, pyridoxal phosphate, lyase
• Biological source: Malus x domestica
• Total number of polymer chains: 1
• Total formula weight: 49891.58

Authors

Capitani, G.,Eliot, A.C.,Gut, H.,Khomutov, R.M.,Kirsch, J.F.,Grutter, M.G. (deposition date: 2002-07-03, release date: 2003-04-22, Last modification date: 2023-10-25)

Primary citation

Capitani, G.,Eliot, A.C.,Gut, H.,Khomutov, R.M.,Kirsch, J.F.,Grutter, M.G.
Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding.
BIOCHEM.BIOPHYS.ACTA PROTEINS & PROTEOMICS, 1647:55-60, 2003

PubMed Abstract: 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.

PubMed: 12686108
DOI: 10.1016/S1570-9639(03)00049-9

Experimental method

X-RAY DIFFRACTION (2.01 Å)