2j2f

From Proteopedia

Revision as of 15:17, 30 October 2007

THE T199D MUTANT OF STEAROYL ACYL CARRIER PROTEIN DESATURASE FROM RICINUS COMMUNIS (CASTOR BEAN)

Overview

Sequence analysis of the diiron cluster-containing soluble desaturases, suggests they are unrelated to other diiron enzymes; however, structural, alignment of the core four-helix bundle of desaturases to other diiron, enzymes reveals a conserved iron binding motif with similar spacing in all, enzymes of this structural class, implying a common evolutionary ancestry., Detailed structural comparison of the castor desaturase with that of a, peroxidase, rubrerythrin, shows remarkable conservation of both identity, and geometry of residues surrounding the diiron center, with the exception, of residue 199. Position 199 is occupied by a threonine in the castor, desaturase, but the equivalent position in rubrerythrin contains a, glutamic acid. We previously hypothesized that a carboxylate in ... [(full description)]

About this Structure

2J2F is a [Single protein] structure of sequence from [Ricinus communis] with FE as [ligand]. Active as [Transferred entry: 1.14.19.2], with EC number [1.14.99.6]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

A single mutation in the castor Delta9-18:0-desaturase changes reaction partitioning from desaturation to oxidase chemistry., Guy JE, Abreu IA, Moche M, Lindqvist Y, Whittle E, Shanklin J, Proc Natl Acad Sci U S A. 2006 Nov 14;103(46):17220-4. Epub 2006 Nov 6. PMID:17088542

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