Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative γ-butyrolactone receptor protein from Streptomyces fradiae
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- 作者：Nurhikmah Mohd-Sharif ; Sofiyah Shaibullah ; Vasanthakumar Givajothi ; Cheng-Seng Tan ; Kok Lian Ho ; Aik-Hong Teh ; Syarul Nataqain Baharum ; Jitka Waterman and Chyan Leong Ng
- 关键词：Streptomyces fradiae ; recombinant TylP protein ; &gamma ; -butyrolactone ; GBL ; transcription factors ; tylosin
- 刊名：Acta Crystallographica Section F
- 出版年：2017
- 出版时间：February 2017
- 年：2017
- 卷：73
- 期：2
- 页码：109-115
- 全文大小：1178K
- ISSN：1744-3091
文摘
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 P3121, with unit-cell parameters a = b = 126.62, c = 95.63 Å.