Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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 E, Bingman CA, Allard ST, Wesenberg GE, Aceti DJ, Wrobel RL, Frederick RO, Sreenath H, Vojtik FC, Jeon WB, Newman CS, Primm J, Sussman MR, Fox BG, Markley JL, Phillips GN Jr Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 May 1;61(Pt, 5):469-72. Epub 2005 Apr 26. PMID:16511070[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bitto E, Bingman CA, Allard ST, Wesenberg GE, Aceti DJ, Wrobel RL, Frederick RO, Sreenath H, Vojtik FC, Jeon WB, Newman CS, Primm J, Sussman MR, Fox BG, Markley JL, Phillips GN Jr. 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. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 May 1;61(Pt, 5):469-72. Epub 2005 Apr 26. PMID:16511070 doi:http://dx.doi.org/10.1107/S1744309105011565
