2apj

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Revision as of 06:09, 21 November 2007

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spinqualitylabelsall models 2apj, resolution 1.600Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

X-Ray Structure of Protein from Arabidopsis Thaliana AT4G34215 at 1.6 Angstrom Resolution

Overview

The crystal structure of the At4g34215 protein of Arabidopsis thaliana was, determined by molecular replacement and refined to an R factor of 14.6%, (R(free) = 18.3%) at 1.6 Angstroms resolution. The crystal structure, confirms that At4g34215 belongs to the SGNH-hydrolase superfamily of, enzymes. The catalytic triad of the enzyme comprises residues Ser31, His238 and Asp235. In this structure the catalytic serine residue was, found to be covalently modified, possibly by phenylmethylsulfonyl, fluoride. The structure also reveals a previously undescribed variation, within the active site. The conserved asparagine from block III, which, provides a hydrogen bond for an oxyanion hole in the SGNH-hydrolase, superfamily enzymes, is missing in At4g34215 and is functionally replaced, by Gln30 from block I. This residue is positioned in a catalytically, competent conformation by nearby residues, including Gln159, Gly160 and, Glu161, which are fully conserved in the carbohydrate esterase family 6, enzymes.

About this Structure

2APJ is a Single protein structure of sequence from Arabidopsis thaliana. This structure superseeds the now removed PDB entry 2AEA. Full crystallographic information is available from OCA.

Reference

The structure at 1.6 Angstroms resolution of the protein product of the At4g34215 gene from Arabidopsis thaliana., Bitto E, Bingman CA, McCoy JG, Allard ST, Wesenberg GE, Phillips GN Jr, Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1655-61. Epub 2005, Nov 19. PMID:16301800

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