1w9y

From Proteopedia

Revision as of 15:24, 5 November 2007

THE STRUCTURE OF ACC OXIDASE

Overview

The final step in the biosynthesis of the plant signaling molecule, ethylene is catalyzed by 1-aminocyclopropane-1-carboxylic acid oxidase, (ACCO). ACCO requires bicarbonate as an activator and catalyzes the, oxidation of ACC to give ethylene, CO2, and HCN. We report crystal, structures of ACCO in apo-form (2.1 A resolution) and complexed with, Fe(II) (2.55 A) or Co(II) (2.4 A). The active site contains a single, Fe(II) ligated by three residues (His177, Asp179, and His234), and it is, relatively open compared to those of the 2-oxoglutarate oxygenases. The, side chains of Arg175 and Arg244, proposed to be involved in binding, bicarbonate, project away from the active site, but conformational changes, may allow either or both to enter the active site. The structures will, form a basis for future mechanistic and inhibition studies.

About this Structure

1W9Y is a Single protein structure of sequence from Petunia x hybrida with SO4 as ligand. Active as Aminocyclopropanecarboxylate oxidase, with EC number 1.14.17.4 Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme., Zhang Z, Ren JS, Clifton IJ, Schofield CJ, Chem Biol. 2004 Oct;11(10):1383-94. PMID:15489165

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