TY - JOUR
T1 - Crystal structure of chondroitin polymerase from Escherichia coli K4
AU - Osawa, Takuo
AU - Sugiura, Nobuo
AU - Shimada, Hiroaki
AU - Hirooka, Ryoko
AU - Tsuji, Atushi
AU - Shirakawa, Tadayoshi
AU - Fukuyama, Keiichi
AU - Kimura, Makoto
AU - Kimata, Koji
AU - Kakuta, Yoshimitsu
N1 - Funding Information:
We thank the staffs of the SPring-8 (beamline 38B1) and the PF (beamline BL5A and NW12A) for help with data collection. This work was supported by a special research fund from the Seikagaku Corporation, and by a Grant-in-Aid for Scientific Research on Priority Areas 14082206 from the Ministry of Education, Culture, Sports, Science, and Technology of Japan. This work was also supported by a research grant from the National Project on Protein Structural and Functional Analyses from the Ministry of Education, Culture, Sports, Science, and Technology of Japan.
PY - 2009/1/2
Y1 - 2009/1/2
N2 - 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.
AB - 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.
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U2 - 10.1016/j.bbrc.2008.08.121
DO - 10.1016/j.bbrc.2008.08.121
M3 - Article
C2 - 18771653
AN - SCOPUS:56949085729
VL - 378
SP - 10
EP - 14
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -