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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.


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.

SUBMITTER: Bitto E 

PROVIDER: S-EPMC1952295 | biostudies-literature | 2005 May

REPOSITORIES: biostudies-literature

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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.

Bitto Eduard E   Bingman Craig A CA   Allard Simon T M ST   Wesenberg Gary E GE   Aceti David J DJ   Wrobel Russell L RL   Frederick Ronnie O RO   Sreenath Hassan H   Vojtik Frank C FC   Jeon Won Bae WB   Newman Craig S CS   Primm John J   Sussman Michael R MR   Fox Brian G BG   Markley John L JL   Phillips George N GN  

Acta crystallographica. Section F, Structural biology and crystallization communications 20050426 Pt 5


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(I  ...[more]

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