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

DOI: 10.1107/S2053230X17001212 DOI Help

Authors: Nurhikmah Mohd-sharif (Universiti Kebangsaan Malaysia) , Sofiyah Shaibullah (Universiti Kebangsaan Malaysia) , Vasanthakumar Givajothi (Universiti Kebangsaan Malaysia) , Cheng-seng Tan (Universiti Kebangsaan Malaysia) , Kok Lian Ho (Universiti Putra Malaysia) , Aik-hong Teh (Universiti Sains Malaysia) , Syarul Nataqain Baharum (Universiti Kebangsaan Malaysia) , Jitka Waterman (Diamond Light Source) , Chyan Leong Ng (Universiti Kebangsaan Malaysia)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 73 , PAGES 109 - 115

State: Published (Approved)
Published: February 2017
Diamond Proposal Number(s): 11175

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 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.

Journal Keywords: Streptomyces fradiae; recombinant TylP protein; γ-butyrolactone; GBL; transcription factors; tylosin

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography