Structure of a halophilic nucleoside diphosphate kinase from Halobacterium salinarum
Structure of a halophilic nucleoside diphosphate kinase from Halobacterium salinarum
复制标题
DOI：
10.1016/j.febslet.2005.10.052
复制
发表时间：
2005-12-05
期刊：
影响因子：
3.5
通讯作者：
Oesterhelt, D
中科院分区：
文献类型：
--
作者：
Besir, H;Zeth, K;Oesterhelt, D
从嗜盐古菌盐杆菌盐的核苷二磷酸激酶结晶在一个自由状态和底物结合的形式与CDP。分别以2.35和2.2埃的分辨率解析结构。用His（6）标记的酶获得具有脱辅基形式的晶体，而未标记的形式用于与核苷酸共结晶。在不同的盐和pH条件下的交联揭示了较强的寡聚化倾向的标记蛋白质在低和高盐浓度。His（6）-标签的嗜盐性质的酶的影响进行了讨论的基础上观察到的结构特性。(c)2005年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
Nucleoside diphosphate kinase from the halophilic archaeon Halobacterium salinarum was crystallized in a free state and a substrate-bound form with CDP. The structures were solved to a resolution of 2.35 and 2.2 angstrom, respectively. Crystals with the apo-form were obtained with His(6)-tagged enzyme, whereas the untagged form was used for co-crystallization with the nucleotide. Crosslinking under different salt and pH conditions revealed a stronger oligomerization tendency for the tagged protein at low and high salt concentrations. The influence of the His(6)-tag on the halophilic nature of the enzyme is discussed on the basis of the observed structural properties. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.