来自弗氏链霉菌的假定γ-丁内酯受体蛋白重组TylP的结晶及X射线晶体学分析。
Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative γ-butyrolactone receptor protein from Streptomyces fradiae.
作者信息
Mohd-Sharif Nurhikmah, Shaibullah Sofiyah, Givajothi Vasanthakumar, Tan Cheng Seng, Ho Kok Lian, Teh Aik Hong, Baharum Syarul Nataqain, Waterman Jitka, Ng Chyan Leong
机构信息
Institute of Systems Biology, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia.
School of Bioscience and Biotechnology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia.
出版信息
Acta Crystallogr F Struct Biol Commun. 2017 Feb 1;73(Pt 2):109-115. doi: 10.1107/S2053230X17001212. Epub 2017 Jan 31.
TylP is one of five regulatory proteins involved in the regulation of antibiotic (tylosin) production, morphological and physiological differentiation in Streptomyces fradiae. Its function is similar to those of various γ-butyrolactone receptor proteins. In this report, N-terminally His-tagged recombinant TylP protein (rTylP) was overproduced in Escherichia coli and purified to homogeneity. The rTylP protein was crystallized from a reservoir solution comprising 34%(v/v) ethylene glycol and 5%(v/v) glycerol. The protein crystals diffracted X-rays to 3.05 Å resolution and belonged to the trigonal space group P321, with unit-cell parameters a = b = 126.62, c = 95.63 Å.
TylP是参与调节弗氏链霉菌中抗生素（泰乐菌素）产生、形态和生理分化的五种调节蛋白之一。其功能类似于各种γ-丁内酯受体蛋白。在本报告中，N端带有组氨酸标签的重组TylP蛋白（rTylP）在大肠杆菌中过量表达并纯化至同质。rTylP蛋白从含有34%（v/v）乙二醇和5%（v/v）甘油的储液中结晶。蛋白质晶体的X射线衍射分辨率为3.05 Å，属于三方晶系空间群P321，晶胞参数a = b = 126.62，c = 95.63 Å。
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