AafA的结晶及初步晶体学分析：肠集聚性大肠杆菌AAF/II菌毛的主要粘附亚基
Crystallization and initial crystallographic analysis of AafA: the major adhesive subunit of the enteroaggregative Escherichia coli AAF/II pilus.
作者信息
Yang Yi, Garnett James A, Matthews Stephen
机构信息
Centre for Structural Biology, Division of Molecular Biosciences, Department of Life Sciences, Imperial College London, South Kensington, London SW7 2AZ, England.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Apr 1;67(Pt 4):454-6. doi: 10.1107/S1744309111001412. Epub 2011 Mar 25.
Abstract
AafA is the major adhesive pilin subunit of the aggregative adherence fimbriae (AAF) from enteroaggregative Escherichia coli, which play an important role by attaching to the host cells during the initial phase of bacterial colonization and invasion. AafA has been crystallized at pH 3.4 and diffraction data have been collected to 2.1 Å resolution. Molecular replacement was unsuccessful and selenomethionine-substituted protein and heavy-atom derivatives are being prepared for phasing.
摘要
AafA是来自肠聚集性大肠杆菌的聚集性黏附菌毛（AAF）的主要黏附菌毛亚基，在细菌定植和侵袭的初始阶段通过附着于宿主细胞发挥重要作用。AafA已在pH 3.4条件下结晶，并收集到了分辨率为2.1 Å的衍射数据。分子置换未成功，目前正在制备硒代甲硫氨酸取代蛋白和重原子衍生物用于相位测定。
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