期刊
STRUCTURE
卷 9, 期 5, 页码 439-450出版社
CELL PRESS
DOI: 10.1016/S0969-2126(01)00604-9
关键词
adenylate intermediate; hinge bending; Rossmann fold; selenomethionine MAD experiment; vitamin B-5
Background: Pantothenate synthetase (EC 6.3.2.1) is the last enzyme of the pathway of pantothenate (vitamin B-5) synthesis. It catalyzes the condensation of pantoate with beta -alanine in an ATP-dependent reaction. Results: We describe the overexpression, purification, and crystal structure of recombinant pantothenate synthetase from E. coli. The structure was solved by a selenomethionine multiwavelength anomalous dispersion experiment and refined against native data to a final R-cryst of 22.6% (R-free = 24.9%) at 1.7 Angstrom resolution. The enzyme is dimeric, with two well-defined domains per protomer: the N-terminal domain, a Rossmann fold, contains the active site cavity, with the C-terminal domain forming a hinged lid. Conclusions: The N-terminal domain is structurally very similar to class I aminoacyl-tRNA synthetases and is thus a member of the cytidylyltransferase superfamily. This relationship has been used to suggest the location of the ATP and pantoate binding sites and the nature of hinge bending that leads to the ternary enzyme-pantoate-ATP complex.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据