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

Research output: Contribution to journalArticlepeer-review

66 Citations (Scopus)


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 languageEnglish
Pages (from-to)10-14
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - Jan 2 2009

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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