title: Structural basis for reduced activity of 1-aminocyclopropane-1-carboxylate synthase affected by a mutation linked to andromonoecy.
abstract: 1-aminocyclopropane-1-carboxylate synthase (ACS) is a key enzyme in the biosynthesis of the plant hormone ethylene. Recently, a new biological role for ACS has been found in Cucumis melo where a single point mutation (A57V) of one isoform of the enzyme, causing reduced activity, results in andromonoecious plants. We present here a straightforward structural basis for the reduced activity of the A57V mutant, based on our work on Malus domestica ACS, including a new structure of the unliganded apple enzyme at 1.35Å resolution.
authors.affiliation: Biomolecular Research, Paul Scherrer Institut, Villigen PSI, Switzerland.
authors.forename: Martin A
authors.initials: MA
authors.lastname: Schärer
authors.forename: Andrew C
authors.initials: AC
authors.lastname: Eliot
authors.forename: Markus G
authors.initials: MG
authors.lastname: Grütter
authors.forename: Guido
authors.initials: G
authors.lastname: Capitani
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D008190:Lyases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D027845:Malus / Q000201:enzymology / Q000235:genetics*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
chemical_list: D010940:Plant Proteins; D008190:Lyases; C021773:1-aminocyclopropanecarboxylate synthase