Format

Send to

Choose Destination
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 May 1;61(Pt 5):469-72. Epub 2005 Apr 26.

The structure at 2.4 A resolution of the protein from gene locus At3g21360, a putative Fe(II)/2-oxoglutarate-dependent enzyme from Arabidopsis thaliana.

Author information

1
Center for Eukaryotic Structural Genomics, Department of Biochemistry, University of Wisconsin-Madison, USA.

Abstract

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% (Rfree = 24.1%) at 2.4 A 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.

PMID:
16511070
PMCID:
PMC1952295
DOI:
10.1107/S1744309105011565
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for International Union of Crystallography Icon for PubMed Central
Loading ...
Support Center