1b8g | pdb_00001b8g
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| 1b8g, resolution 2.37Å | |||||||||||||
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| Ligands: | PLP | ||||||||||||
| Activity: | 1-aminocyclopropane-1-carboxylate synthase, with EC number 4.4.1.14 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE
Overview
The 2.4 A crystal structure of the vitamin B6-dependent enzyme 1-aminocyclopropane-1-carboxylate (ACC) synthase is described. This enzyme catalyses the committed step in the biosynthesis of ethylene, a plant hormone that is responsible for the initiation of fruit ripening and for regulating many other developmental processes. ACC synthase has 15 % sequence identity with the well-studied aspartate aminotransferase, and a completely different catalytic activity yet the overall folds and the active sites are very similar. The new structure together with available biochemical data enables a comparative mechanistic analysis that largely explains the catalytic roles of the conserved and non-conserved active site residues. An external aldimine reaction intermediate (external aldimine with ACC, i.e. with the product) has been modeled. The new structure provides a basis for the rational design of inhibitors with broad agricultural applications.
About this Structure
1B8G is a Single protein structure of sequence from Malus x domestica. Full crystallographic information is available from OCA.
Reference
Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene., Capitani G, Hohenester E, Feng L, Storici P, Kirsch JF, Jansonius JN, J Mol Biol. 1999 Dec 3;294(3):745-56. PMID:10610793
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