Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative γ-butyrolactone receptor protein from Streptomyces fradiae

被引：4
|
作者：
Mohd-Sharif, Nurhikmah [1 ]
Shaibullah, Sofiyah [1 ]
Givajothi, Vasanthakumar [2 ]
Tan, Cheng-Seng [2 ]
Ho, Kok Lian [3 ]
Teh, Aik-Hong [4 ]
Baharum, Syarul Nataqain [1 ]
Waterman, Jitka [5 ]
Ng, Chyan Leong [1 ]
机构：
[1] Univ Kebangsaan Malaysia, Inst Syst Biol, Ukm Bangi 43600, Selangor, Malaysia
[2] Univ Kebangsaan Malaysia, Sch Biosci & Biotechnol, Fac Sci & Technol, Ukm Bangi 43600, Selangor, Malaysia
[3] Univ Putra Malaysia, Dept Pathol, Fac Med & Hlth Sci, Upm Serdang 43400, Selangor, Malaysia
[4] Univ Sains Malaysia, Ctr Chem Biol, 10 Persiaran Bukit Jambul, Bayan Lepas 11900, Penang, Malaysia
[5] Diamond Light Source, Harwell Sci & Innovat Campus, Didcot OX11 0DE, Oxon, England
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2017年 / 73卷
关键词：
Streptomyces fradiae; recombinantTylP protein; gamma-butyrolactone; GBL; transcription factors; tylosin; AUTOREGULATOR RECEPTOR; TETR FAMILY; A-FACTOR; SECONDARY METABOLISM; FUNCTIONAL-ANALYSIS; TRANSCRIPTIONAL REGULATORS; MOLECULAR REPLACEMENT; MICROBIAL HORMONE; COELICOLOR A3(2); STRUCTURAL BASIS;
D O I：
10.1107/S2053230X17001212
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
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 gamma-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 angstrom resolution and belonged to the trigonal space group P3(1)21, with unit-cell parameters a = b = 126.62, c = 95.63 angstrom.
引用
收藏
页码：109 / 115
页数：7
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