The structure at 2.4 Å resolution of the protein from gene locus At3g21360, a putative FeII/2-oxoglutaratedependent enzyme from Arabidopsis thaliana
The structure at 2.4 Å resolution of the protein from gene locus At3g21360, a putative FeII/2-oxoglutaratedependent enzyme from Arabidopsis thaliana
复制标题
DOI：
10.1107/s1744309105011565
复制
发表时间：
2005-05-01
影响因子：
0.9
通讯作者：
Phillips, GN
中科院分区：
文献类型：
--
作者：
Bitto, E;Bingman, CA;Phillips, GN
用单波长反常色散法测定了拟南芥AT3g21360基因产物的晶体结构，在2.4埃分辨率下，R因子为19.3%(无R=24.1%)。晶体结构包括不对称单元中的两个单体，它们在跨越残基178-230的柔性结构域的构象上不同。晶体结构证实，At3g21360编码一个属于棒状合成酶样铁(II)和2-氧戊二酸依赖酶超家族的蛋白质。金属结合位点被定义并且类似于在超家族的其他成员中发现的铁(II)结合位点。
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% (R-free = 24.1%) at 2.4 angstrom 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.