脑膜炎奈瑟菌冷休克结构域蛋白的结构揭示了一种链交换二聚体。
Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer.
作者信息
Ren Jingshan, Nettleship Joanne E, Sainsbury Sarah, Saunders Nigel J, Owens Raymond J
机构信息
The Oxford Protein Production Facility, Henry Wellcome Building for Genomic Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, England.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Apr 1;64(Pt 4):247-51. doi: 10.1107/S1744309108005411. Epub 2008 Mar 21.
Abstract
The structure of the cold-shock domain protein from Neisseria meningitidis has been solved to 2.6 A resolution and shown to comprise a dimer formed by the exchange of two beta-strands between protein monomers. The overall fold of the monomer closely resembles those of other bacterial cold-shock proteins. The neisserial protein behaved as a monomer in solution and was shown to bind to a hexathymidine oligonucleotide with a stoichiometry of 1:1 and a K(d) of 1.25 microM.
摘要
脑膜炎奈瑟菌冷休克结构域蛋白的结构已解析至2.6埃分辨率，显示为由蛋白单体之间两条β链交换形成的二聚体。单体的整体折叠与其他细菌冷休克蛋白的折叠非常相似。奈瑟菌蛋白在溶液中表现为单体，并显示以1:1的化学计量比和1.25微摩尔的解离常数（K(d)）与六聚胸苷寡核苷酸结合。
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