Open AccessThe structure at 2.4 Å resolution of the protein from gene locus At3g21360, a putative Fe II /2‐oxoglutarate‐dependent enzyme from Arabidopsis thaliana
Author(s) -
Bitto Eduard,
Bingman Craig A.,
Aceti David J.,
Allard Simon T. M.,
Wesenberg Gary E.,
Wrobel Russell L.,
Frederick Ronnie O.,
Vojtik Frank C.,
Sreenath Hassan,
Jeon Won Bae,
Newman Craig S.,
Primm John,
Sussman Michael R.,
Fox Brian G.,
Markley John L.,
Phillips George N.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105011565
Subject(s) - arabidopsis thaliana , crystal structure , gene , chemistry , locus (genetics) , stereochemistry , superfamily , arabidopsis , crystallography , enzyme , oxidoreductase , biology , biochemistry , mutant
The crystal structure of the gene product of At3g21360 from Arabidopsis thaliana was determined by the single‐wavelength anomalous dispersion method and refined to an R factor of 19.3% ( R free = 24.1%) at 2.4 Å resolution. The crystal structure includes two monomers in the asymmetric unit that differ in the conformation of a flexible domain that spans residues 178–230. The crystal structure confirmed that At3g21360 encodes a protein belonging to the clavaminate synthase‐like superfamily of iron(II) and 2‐oxoglutarate‐dependent enzymes. The metal‐binding site was defined and is similar to the iron(II) binding sites found in other members of the superfamily.