大西洋鳕鱼（Gadus morhua）冷适应尿嘧啶-DNA糖基化酶的结晶及初步X射线衍射分析

Crystallization and preliminary X-ray diffraction analysis of a cold-adapted uracil-DNA glycosylase from Atlantic cod (Gadus morhua).

作者信息

Leiros I, Lanes O, Sundheim O, Helland R, Smalås A O, Willassen N P

机构信息

Department of Chemistry, Faculty of Science, University of Tromsø, N-9037 Tromsø, Norway.

出版信息

Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1706-8. doi: 10.1107/s0907444901013427. Epub 2001 Oct 25.

DOI:10.1107/s0907444901013427

PMID:11679752

Abstract

Uracil-DNA glycosylase (UDG) is a DNA-repair enzyme involved in the removal of uracil from DNA. The Atlantic cod UDG (cUDG) possesses typical cold-adaptation features, with higher catalytic efficiency and lower thermal stability than the mammalian counterparts. cUDG has been crystallized by the vapour-diffusion method using sodium citrate as the precipitant at pH 7.5. The crystals are monoclinic and belong to space group P2(1), with unit-cell parameters a = 68.58, b = 67.19, c = 68.64 A, beta = 119.85 degrees. There are two molecules in the asymmetric unit, with a corresponding V(M) value of 2.71 A(3) Da(-1) and a solvent content of 54.7%. Synchrotron diffraction data have been collected to 1.9 A resolution using cryogenic conditions (120 K).

摘要

尿嘧啶-DNA糖基化酶（UDG）是一种参与从DNA中去除尿嘧啶的DNA修复酶。大西洋鳕鱼UDG（cUDG）具有典型的冷适应特征，与哺乳动物的同类酶相比，具有更高的催化效率和更低的热稳定性。cUDG已通过气相扩散法，以柠檬酸钠作为沉淀剂，在pH 7.5条件下结晶。晶体为单斜晶系，属于空间群P2(1)，晶胞参数a = 68.58、b = 67.19、c = 68.64 Å，β = 119.85°。不对称单元中有两个分子，相应的V(M)值为2.71 Å³ Da⁻¹，溶剂含量为54.7%。已在低温条件（120 K）下收集到分辨率为1.9 Å的同步辐射衍射数据。