Crystal structure of chondroitin polymerase from Escherichia coli K4

Takuo Osawa, Nobuo Sugiura, Hiroaki Shimada, Ryoko Hirooka, Atushi Tsuji, Tadayoshi Shirakawa, Keiichi Fukuyama, Makoto Kimura, Koji Kimata, Yoshimitsu Kakuta

研究成果: ジャーナルへの寄稿記事

43 引用 (Scopus)

抄録

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.

元の言語英語
ページ(範囲)10-14
ページ数5
ジャーナルBiochemical and Biophysical Research Communications
378
発行部数1
DOI
出版物ステータス出版済み - 1 2 2009

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Chondroitin
Uridine Diphosphate
Escherichia coli
Crystal structure
Elongation
Catalytic Domain
Glycosyltransferases
Biosynthesis
Glycosaminoglycans

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

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.

:: Biochemical and Biophysical Research Communications, 巻 378, 番号 1, 02.01.2009, p. 10-14.

研究成果: ジャーナルへの寄稿記事

Osawa, T, Sugiura, N, Shimada, H, Hirooka, R, Tsuji, A, Shirakawa, T, Fukuyama, K, Kimura, M, Kimata, K & Kakuta, Y 2009, 'Crystal structure of chondroitin polymerase from Escherichia coli K4', Biochemical and Biophysical Research Communications, 巻. 378, 番号 1, pp. 10-14. https://doi.org/10.1016/j.bbrc.2008.08.121
Osawa, Takuo ; Sugiura, Nobuo ; Shimada, Hiroaki ; Hirooka, Ryoko ; Tsuji, Atushi ; Shirakawa, Tadayoshi ; Fukuyama, Keiichi ; Kimura, Makoto ; Kimata, Koji ; Kakuta, Yoshimitsu. / Crystal structure of chondroitin polymerase from Escherichia coli K4. :: Biochemical and Biophysical Research Communications. 2009 ; 巻 378, 番号 1. pp. 10-14.
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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 {\AA} 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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AU - Sugiura, Nobuo

AU - Shimada, Hiroaki

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AU - Tsuji, Atushi

AU - Shirakawa, Tadayoshi

AU - Fukuyama, Keiichi

AU - Kimura, Makoto

AU - Kimata, Koji

AU - Kakuta, Yoshimitsu

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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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