2brj
From Proteopedia
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X-RAY STRUCTURE OF THE ALLENE OXIDE CYCLASE FROM ARABIDOPSIS THALIANA
Overview
We describe the crystallization and structure elucidation of Arabidopsis, thaliana allene oxide cyclase 2 (AOC2), a key enzyme in the biosynthesis, of jasmonates. In a coupled reaction with allene oxide synthase, AOC2, releases the first cyclic and biologically active metabolite, 12-oxo-phytodienoic acid (OPDA). AOC2 (AT3G25770) folds into an, eight-stranded antiparallel beta-barrel with a C-terminal partial helical, extension. The protein forms a hydrophobic binding cavity with two, distinct polar patches. AOC2 is trimeric in crystals, in vitro and in, planta. Based on the observed folding pattern, we assigned AOC2 as a low, molecular weight member of the lipocalin family with enzymatic activity in, plants. We determined the binding position of the competitive inhibitor, vernolic acid (a ... [(full description)]
About this Structure
2BRJ is a [Single protein] structure of sequence from [Arabidopsis thaliana] with GOL as [ligand]. Active as [[1]], with EC number [5.3.99.6]. Full crystallographic information is available from [OCA].
Reference
The crystal structure of Arabidopsis thaliana allene oxide cyclase: insights into the oxylipin cyclization reaction., Hofmann E, Zerbe P, Schaller F, Plant Cell. 2006 Nov;18(11):3201-17. Epub 2006 Nov 3. PMID:17085685
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