1B8G: 1-aminocyclopropane-1-carboxylate Synthase

Citation:
Abstract
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.
PDB ID: 1B8GDownload
MMDB ID: 12342
PDB Deposition Date: 1999/1/31
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.37  Å
Source Organism:
Similar Structures:
Biological Unit for 1B8G: dimeric; determined by author and by software (PISA,PQS)
Molecular Components in 1B8G
Label Count Molecule
Proteins (2 molecules)
2
Protein (1-aminocyclopropane-1-carboxylate Synthase)
Molecule annotation
Chemicals (2 molecules)
1
2
* Click molecule labels to explore molecular sequence information.

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