Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding.
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.
Capitani
Guido
G
Biochemisches Institut der Universität Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland. capitani@bioc.unizh.ch
Eliot
Andrew C
AC
Gut
Heinz
H
Khomutov
Radii M
RM
Kirsch
Jack F
JF
Grütter
Markus G
MG
D018360:Crystallography, X-Ray; D008190:Lyases / Q000737:chemistry*; D011487:Protein Conformation; D011732:Pyridoxal Phosphate / Q000737:chemistry; D013452:Sulfonium Compounds / Q000737:chemistry
D013452:Sulfonium Compounds; D011732:Pyridoxal Phosphate; D008190:Lyases; C021773:1-aminocyclopropanecarboxylate synthase