3PIU

High-resolution structure of native Malus domestica ACC synthase

Summary for 3PIU

• Entry DOI: 10.2210/pdb3piu/pdb
• Descriptor: 1-aminocyclopropane-1-carboxylate synthase, (5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL DIHYDROGEN PHOSPHATE (3 entities in total)
• Functional Keywords: fruit ripening, ethylene biosynthesis, lyase, pyridoxal 5'-phosphate binding
• Biological source: Malus domestica (apple)
• Total number of polymer chains: 1
• Total formula weight: 49553.07

Authors

Scharer, M.A.,Grutter, M.G.,Capitani, G. (deposition date: 2010-11-08, release date: 2010-12-15, Last modification date: 2023-12-06)

Primary citation

Scharer, M.A.,Eliot, A.C.,Grutter, M.G.,Capitani, G.
Structural basis for reduced activity of 1-aminocyclopropane-1-carboxylate synthase affected by a mutation linked to andromonoecy.
Febs Lett., 585:111-114, 2011

PubMed 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.

PubMed: 21075107
DOI: 10.1016/j.febslet.2010.11.013

Experimental method

X-RAY DIFFRACTION (1.35 Å)