大肠杆菌铁超氧化物歧化酶在3.1埃分辨率下的结构：在单体和二聚体水平上均与铜/锌蛋白结构不同。
Iron superoxide dismutase from Escherichia coli at 3.1-A resolution: a structure unlike that of copper/zinc protein at both monomer and dimer levels.
作者信息
Stallings W C, Powers T B, Pattridge K A, Fee J A, Ludwig M L
出版信息
Proc Natl Acad Sci U S A. 1983 Jul;80(13):3884-8. doi: 10.1073/pnas.80.13.3884.
Abstract
The structure of iron superoxide dismutase (EC 1.15.1.1) from Escherichia coli has been determined at 3.1-A resolution. The dimeric molecule is constructed from identical subunits, which are two-domain polypeptides. The NH2-terminal domain is composed of two antiparallel crossing helices and the COOH-terminal domain is a three-layered structure characterized by mixed alpha/beta secondary structural features. The active center iron atoms, separated by 18 A and located near the monomer-monomer interface, are coordinated by two amino acid residues from each domain. Azide binding has been investigated by using difference Fourier techniques. Consistent with the notion of the independent evolution of the copper/zinc dismutase gene, the iron dismutase structure resembles the copper/zinc protein at neither the monomer nor the dimer level.
摘要
已通过3.1埃的分辨率确定了来自大肠杆菌的铁超氧化物歧化酶（EC 1.15.1.1）的结构。二聚体分子由相同的亚基构成，这些亚基是两结构域的多肽。NH2端结构域由两个反平行交叉螺旋组成，COOH端结构域是具有混合α/β二级结构特征的三层结构。活性中心的铁原子相距18埃，位于单体-单体界面附近，由每个结构域的两个氨基酸残基配位。已使用差分傅里叶技术研究了叠氮化物的结合。与铜/锌歧化酶基因独立进化的观点一致，铁歧化酶的结构在单体水平和二聚体水平上均与铜/锌蛋白不同。
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