3-DIMENSIONAL STRUCTURE OF BACTERIAL LUCIFERASE FROM VIBRIO-HARVEYI AT 2.4 ANGSTROM RESOLUTION
3-DIMENSIONAL STRUCTURE OF BACTERIAL LUCIFERASE FROM VIBRIO-HARVEYI AT 2.4 ANGSTROM RESOLUTION
复制标题
DOI：
10.1021/bi00020a002
复制
发表时间：
1995-05-23
期刊：
影响因子：
2.9
通讯作者：
RAYMENT, I
中科院分区：
文献类型：
--
作者：
FISHER, AJ;RAUSHEL, FM;RAYMENT, I
荧光素酶是一类在可见光光谱中产生光的酶。来自发光海洋细菌的荧光素酶是一种α-β异二聚体单加氧酶，催化FMNH(2)和长链脂肪醛的氧化。哈维氏弧菌细菌荧光素酶的X射线晶体结构已测定到2.4埃分辨率。通过不对称单元中两个杂二聚体之间的多次同象取代和分子平均相结合的方法解决了结构问题。每个亚基折叠成(β/α)(8)桶基序，二聚化通过以伪2折叠ASIS为中心的平行四螺旋束介导，该ASIS将结构相似的亚基联系在一起。通过与相似的蛋白质基序的相关性和以前的生化研究，已经在阿尔法亚基上确定了活性部位的附近，这里给出的结构代表了生物发光酶的第一个分子模型。
Luciferases are a class of enzymes that generate light in the visible spectrum. Luciferase from luminous marine bacteria is an alpha-beta heterodimer monooxygenase that catalyzes the oxidation of FMNH(2) and a long-chain aliphatic aldehyde. The X-ray crystal structure of bacterial luciferase from Vibrio harveyi has been determined to 2.4 Angstrom resolution. The structure was solved by a combination of multiple isomorphous replacement and molecular averaging between the two heterodimers in the asymmetric unit. Each subunit folds into a (beta/alpha)(8) barrel motif, and dimerization is mediated through a parallel four-helix bundle centered on a pseudo 2-fold asis that relates the structurally similar subunits. The vicinity of the active site has been identified on the alpha subunit by correlations with similar protein motifs and previous biochemical studies, The structure presented here represents the first molecular model of a bioluminescent enzyme.