Beich-Frandsen Mads, Večerek Branislav, Sjöblom Björn, Bläsi Udo, Djinović-Carugo Kristina
Department of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt 5):536-40. doi: 10.1107/S174430911100786X. Epub 2011 Apr 20.
The structure of full-length host factor Qβ (Hfq) from Escherichia coli obtained from a crystal belonging to space group P1, with unit-cell parameters a = 61.91, b = 62.15, c = 81.26 Å, α = 78.6, β = 86.2, γ = 59.9°, was solved by molecular replacement to a resolution of 2.85 Å and refined to R(work) and R(free) values of 20.7% and 25.0%, respectively. Hfq from E. coli has previously been crystallized and the structure has been solved for the N-terminal 72 amino acids, which cover ~65% of the full-length sequence. Here, the purification, crystallization and structural data of the full 102-amino-acid protein are presented. These data revealed that the presence of the C-terminus changes the crystal packing of E. coli Hfq. The crystal structure is discussed in the context of the recently published solution structure of Hfq from E. coli.
通过分子置换法解析了来源于大肠杆菌的全长宿主因子Qβ（Hfq）的结构，该晶体属于P1空间群，晶胞参数为a = 61.91、b = 62.15、c = 81.26 Å，α = 78.6°、β = 86.2°、γ = 59.9°，分辨率为2.85 Å，最终的R(work)和R(free)值分别为20.7%和25.0%。此前已获得大肠杆菌Hfq的晶体，并解析了其N端72个氨基酸的结构，该片段覆盖了全长序列的约65%。本文给出了完整的102个氨基酸的蛋白质的纯化、结晶及结构数据。这些数据表明，C端的存在改变了大肠杆菌Hfq的晶体堆积方式。结合最近发表的大肠杆菌Hfq的溶液结构对晶体结构进行了讨论。
