| Literature DB >> 16511070 |
Eduard Bitto1, Craig A Bingman, Simon T M Allard, Gary E Wesenberg, David J Aceti, Russell L Wrobel, Ronnie O Frederick, Hassan Sreenath, Frank C Vojtik, Won Bae Jeon, Craig S Newman, John Primm, Michael R Sussman, Brian G Fox, John L Markley, George N Phillips.
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.Entities:
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Year: 2005 PMID: 16511070 PMCID: PMC1952295 DOI: 10.1107/S1744309105011565
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091