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Crystal structure of chondroitin polymerase from Escherichia coli K4 |
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| Authors: | Osawa Takuo Sugiura Nobuo Shimada Hiroaki Hirooka Ryoko Tsuji Atushi Shirakawa Tadayoshi Fukuyama Keiichi Kimura Makoto Kimata Koji Kakuta Yoshimitsu |
| Affiliation: | a Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University, Fukuoka 812-8581, Japan b Institute for Molecular Science of Medicine, Aichi Medical University, Yazako, Nagakute, Aichi 480-1195, Japan c Central Research Laboratories, Seikagaku Corporation, Tateno, Higashiyamato-shi, Tokyo 207-0021, Japan d Laboratory of Biochemistry, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, 6-10-1, Hakozaki, Higashi-ku, Fukuoka 812-8581, Japan e Department of Biological Sciences, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan |
| Abstract: | Elongation of glycosaminoglycan chains, such as heparan and chondroitin, is catalyzed by bi-functional glycosyltransferases, for which both 3-dimensional structures and reaction mechanisms remain unknown. The bacterial chondroitin polymerase K4CP catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. Here, we have determined the crystal structure of K4CP in the presence of UDP and UDP-GalNAc as well as with UDP and UDP-GlcUA. The structures consisted of two GT-A fold domains in which the two active sites were 60 Å apart. UDP-GalNAc and UDP-GlcUA were found at the active sites of the N-terminal and C-terminal domains, respectively. The present K4CPstructures have provided the structural basis for further investigating the molecular mechanism of biosynthesis of chondroitin chain. |
| Keywords: | Bi-functional glycosyltransferases Crystal structure Chondroitin polymerase Biosynthesis of chondroitin Biosynthesis of glycosaminoglycan |
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