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.
| Original language | English |
|---|---|
| Pages (from-to) | 10-14 |
| Number of pages | 5 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 378 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Jan 2 2009 |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
Crystal structure of chondroitin polymerase from Escherichia coli K4. / Osawa, Takuo; Sugiura, Nobuo; Shimada, Hiroaki; Hirooka, Ryoko; Tsuji, Atushi; Shirakawa, Tadayoshi; Fukuyama, Keiichi; Kimura, Makoto; Kimata, Koji; Kakuta, Yoshimitsu.
In: Biochemical and Biophysical Research Communications, Vol. 378, No. 1, 02.01.2009, p. 10-14.Research output: Contribution to journal › Article
}
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
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
VL - 378
SP - 10
EP - 14
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -