Structural basis for reduced activity of 1-aminocyclopropane-1-carboxylate synthase affected by a mutation linked to andromonoecy |
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| Authors: | Schärer Martin A Eliot Andrew C Grütter Markus G Capitani Guido |
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| Institution: | aBiomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland;bDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3206, USA;cDepartment of Biochemistry, University of Zurich, CH-8057 Zurich, Switzerland |
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| 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 1.35 Å resolution. |
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| Keywords: | 1-aminocyclopropane-1-carboxylate synthase Pyridoxal 5&prime -phosphate Andromonoecy Ethylene signalling Protein crystallography Comparative modelling |
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