Literature DB >> 16511070

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.

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.

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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


  23 in total

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