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On the interaction site of serine acetyltransferase in the cysteine synthase complex from Escherichia coli |
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| Authors: | Zhao Chunhui Moriga Yudai Feng Bin Kumada Yoichi Imanaka Hiroyuki Imamura Koreyoshi Nakanishi Kazuhiro |
| Institution: | Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University, 3-1-1 Tsushima-naka, Okayama 700-8530, Japan. |
| Abstract: | Cysteine synthase from Escherichia coli is a bienzyme complex comprised of serine acetyltransferase (SAT) and O-acetylserine sulfhydrylase A. The site of interaction of a SAT molecule was investigated by gel chromatography and surface plasmon technique using various mutant-type SATs, to better understand the mechanism involved in complex formation. The C-terminus of SAT, Ile 273, along with Glu 268 and Asp 271, was found to be essential for complex formation. The effects of O-acetyl-L-serine and sulfide on the affinity for the complex formation were also studied using a surface plasmon technique. |
| Keywords: | Serine acetyltransferase O-Acetylserine sulfhydrylase Cysteine synthase Protein-protein interaction Surface plasmon resonance |
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