Binding study of AfsK, a Ser/Thr kinase from Streptomyces coelicolor A3(2) and S-adenosyl-L-methionine.
Streptomyces coelicolor A3(2) produces an antibiotic, actinorhodin, which belongs to the aromatic polyketides and which can function as an acid/base indicator. Its production results in the death of microorganisms in the vicinity of S. coelicolor A3(2), and this phenomenon can be used in concert with biopesticides. The exogenous addition of S-adenosyl-L-methionine (SAM) to S. coelicolor A3(2) enhances its actinorhodin production and may initiate actinorhodin biosynthesis, with at least four genes being involved. Of these (because afsK initiates the others), AfsK, the protein expressed from afsK, may be interacting with SAM. Although the three-dimensional structure of AfsK has not been determined, the differences between nuclear magnetic resonance (NMR) signals obtained from the free form of SAM and those from a SAM-protein complex can help us to determine whether SAM binds to the C-terminal of AfsK or not. In the present study, NMR data analysis strongly supported the idea that SAM binds to AfsK.
Lee
Yukyung
Y
Bio/Molecular Informatics Center, IBST, Department of Bioscience and Biotechnology, Konkuk University, Seoul, Korea.
Kim
Kwangsoo
K
Suh
Joo-Won
JW
Rhee
Sangkee
S
Lim
Yoongho
Y
D000880:Anthraquinones / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D015964:Gene Expression Regulation, Bacterial / Q000187:drug effects; D009682:Magnetic Resonance Spectroscopy; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D012436:S-Adenosylmethionine / Q000494:pharmacology*; D048372:Streptomyces coelicolor / Q000235:genetics / Q000378:metabolism*; D000095622:Benzoisochromanequinones
D000880:Anthraquinones; D001426:Bacterial Proteins; D017346:Protein Serine-Threonine Kinases; D012436:S-Adenosylmethionine; C013390:actinorhodin; D000095622:Benzoisochromanequinones