核糖体失活蛋白β-丝瓜素在2.0埃分辨率下的晶体结构。

Crystal structure of beta-luffin, a ribosome-inactivating protein, at 2.0 A resolution.

作者信息

Ma Qing-Jun, Li Jian-Hui, Li Hui Guang, Wu Shen, Dong Yi-Cheng

机构信息

Center for Molecular Biology, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, People's Republic of China.

出版信息

Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1366-70. doi: 10.1107/s0907444903011156. Epub 2003 Jul 23.

DOI:10.1107/s0907444903011156

PMID:12876337

Abstract

The crystal structure of beta-luffin at 2.0 A resolution was solved by the molecular-replacement method using polyalanyl trichosanthin as the search model. The structure was refined with CNS1.1, giving R(work) = 0.162 and R(free) = 0.204. The r.m.s.d.s of the bond lengths and bond angles are 0.008 A and 1.3 degrees, respectively. The overall structure is similar to those of other type I RIPs. Three N-acetylglucosamine (Nag) molecules are linked to residues Asn2, Asn78 and Asn85 of the protein.

摘要

采用多聚丙氨酰天花粉蛋白作为搜索模型，通过分子置换法解析了分辨率为2.0 Å的β-丝瓜素晶体结构。使用CNS1.1对该结构进行了精修，得到的R(work) = 0.162，R(free) = 0.204。键长和键角的均方根偏差分别为0.008 Å和1.3°。整体结构与其他I型核糖体失活蛋白相似。三个N-乙酰葡糖胺（Nag）分子与该蛋白的Asn2、Asn78和Asn85残基相连。