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

ABSTRACT: 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 ?-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.

SUBMITTER: Mohd-Sharif N

PROVIDER: S-EPMC5297932 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature

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

Mohd-Sharif Nurhikmah N Shaibullah Sofiyah S Givajothi Vasanthakumar V Tan Cheng Seng CS Ho Kok Lian KL Teh Aik Hong AH Baharum Syarul Nataqain SN Waterman Jitka J Ng Chyan Leong CL

Acta crystallographica. Section F, Structural biology communications 20170131 Pt 2

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/ ...[more]

PMID: 28177322

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