Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative γ-butyrolactone receptor protein from Streptomyces fradiae.
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.
Institute of Systems Biology, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia.
Nurhikmah
N
Mohd-Sharif
Institute of Systems Biology, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia.
Sofiyah
S
Shaibullah
School of Bioscience and Biotechnology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia.
Vasanthakumar
V
Givajothi
School of Bioscience and Biotechnology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia.
Cheng Seng
CS
Tan
Department of Pathology, Faculty of Medicine and Health Sciences, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia.
Kok Lian
KL
Ho
Centre for Chemical Biology, Universiti Sains Malaysia, 10 Persiaran Bukit Jambul, 11900 Bayan Lepas, Penang, Malaysia.
Aik Hong
AH
Teh
Institute of Systems Biology, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia.
Syarul Nataqain
SN
Baharum
Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, England.
Jitka
J
Waterman
Institute of Systems Biology, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia.
Chyan Leong
CL
Ng
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D019855:Ethylene Glycol / Q000737:chemistry; D015870:Gene Expression; D005990:Glycerol / Q000737:chemistry; D010957:Plasmids / Q000737:chemistry / Q000378:metabolism; D000072756:Protein Conformation, alpha-Helical; D011963:Receptors, GABA-A / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013302:Streptomyces / Q000737:chemistry* / Q000378:metabolism; D014961:X-Ray Diffraction
C037481:4-butyrolactone receptor; D001426:Bacterial Proteins; D011963:Receptors, GABA-A; D011994:Recombinant Proteins; D019855:Ethylene Glycol; D005990:Glycerol
GBL; Streptomyces fradiae; recombinant TylP protein; transcription factors; tylosin; γ-butyrolactone