2APJ

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

Replaces:  2AEA

Summary for 2APJ

• Entry DOI: 10.2210/pdb2apj/pdb
• Related: 2AEA
• Descriptor: Putative Esterase (2 entities in total)
• Functional Keywords: at4g34215, putative esterase, sgnh-hydrolase superfamily, carbohydrate esterase family 6, structural genomics, protein structure initiative, psi, cesg, center for eukaryotic structural genomics, unknown function
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 4
• Total formula weight: 114185.69

Authors

Wesenberg, G.E.,Phillips Jr., G.N.,Mccoy, J.G.,Bitto, E.,Bingman, C.A.,Allard, S.T.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2005-08-16, release date: 2005-08-30, Last modification date: 2023-08-23)

Primary citation

Bitto, E.,Bingman, C.A.,McCoy, J.G.,Allard, S.T.,Wesenberg, G.E.,Phillips, G.N.
The structure at 1.6 Angstroms resolution of the protein product of the At4g34215 gene from Arabidopsis thaliana.
Acta Crystallogr.,Sect.D, 61:1655-1661, 2005

PubMed Abstract: 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.

PubMed: 16301800
DOI: 10.1107/S0907444905034074

Experimental method

X-RAY DIFFRACTION (1.6 Å)