来自无乳链球菌的同二聚体GBS1074。
The homodimeric GBS1074 from Streptococcus agalactiae.
作者信息
Shukla Anshuman, Pallen Mark, Anthony Mark, White Scott A
机构信息
School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, England.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Nov 1;66(Pt 11):1421-5. doi: 10.1107/S1744309110036286. Epub 2010 Oct 27.
Abstract
ESAT-6 is a well characterized secreted protein from Mycobacterium tuberculosis and represents the archetype of the WXG100 family of proteins. Genes encoding ESAT-6 homologues have been identified in the genome of the human pathogen Streptococcus agalactiae; one of these genes, esxA, has been cloned and the recombinant protein has been crystallized. In contrast to M. tuberculosis ESAT-6, the crystal structure of GBS1074 reveals a homodimeric structure similar to homologous structures from Staphylococcus aureus and Helicobacter pylori. Intriguingly, GBS1074 forms elongated fibre-like assemblies in the crystal structure.
摘要
早期分泌性抗原靶蛋白6（ESAT-6）是一种来自结核分枝杆菌的特征明确的分泌蛋白，是WXG100蛋白家族的原型。在人类病原体无乳链球菌的基因组中已鉴定出编码ESAT-6同源物的基因；其中一个基因esxA已被克隆，重组蛋白已结晶。与结核分枝杆菌ESAT-6不同，无乳链球菌ESAT-6（GBS1074）的晶体结构显示出与金黄色葡萄球菌和幽门螺杆菌同源结构相似的同型二聚体结构。有趣的是，GBS1074在晶体结构中形成细长的纤维状聚集体。
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