巨大消化链球菌蛋白L单个Fab结合结构域的结晶及X射线分析。

Crystallization and X-ray analysis of a single fab binding domain from protein L of Peptostreptococcus magnus.

作者信息

Sohi M K, Wan T, Sutton B J, Atkinson T, Atkinson M A, Murphy J P, Bottomley S P, Gore M G

机构信息

Biomedical Sciences Division, King's College London, UK.

出版信息

Proteins. 1995 Dec;23(4):610-2. doi: 10.1002/prot.340230420.

DOI:10.1002/prot.340230420

PMID:8749861

Abstract

Protein L is a multidomain cell wall constituent of certain strains of Peptostreptococcus magnus which binds to the variable domain of immunoglobulin kappa-light chains. A single immunoglobulin-binding domain of M(r) = 9000 from this protein has been isolated and crystallized. The crystals are of space group P4(2)2(1)2, with cell dimensions a = b = 66.9 A, c = 68.3 A, and diffract to at least 2.2 A resolution. The asymmetric unit of the crystal contains two molecules of the protein L domain, related by a noncrystallographic 2-fold axis, as revealed by a self-rotation function calculated with native diffraction data.

摘要

L蛋白是某些大消化链球菌菌株的一种多结构域细胞壁成分，它能与免疫球蛋白κ轻链的可变结构域结合。已从该蛋白中分离出一个相对分子质量为9000的单一免疫球蛋白结合结构域并使其结晶。晶体属于空间群P4(2)2(1)2，晶胞参数a = b = 66.9 Å，c = 68.3 Å，衍射分辨率至少为2.2 Å。根据天然衍射数据计算的自旋转函数表明，晶体的不对称单元包含两个L蛋白结构域分子，它们通过一个非晶体学2次轴相关联。