Chitobiose phosphorylase from Vibrio proteolyticus, a member of glycosyl transferase family 36, has a clan GH-L-like (α/α)6 barrel fold

Masafumi Hidaka, Yuji Honda, Motomitsu Kitaoka, Satoru Nirasawa, Kiyoshi Hayashi, Takayoshi Wakagi, Hirofumi Shoun, Shinya Fushinobu

Research output: Contribution to journalArticlepeer-review

74 Citations (Scopus)

Abstract

Vibrio proteolyticus chitobiose phosphorylase (ChBP) belongs to glycosyl transferase family 36 (GT-36), and catalyzes the reversible phosphorolysis of chitobiose into α-GlcNAc-1-phosphate and GlcNAc with inversion of the anomeric configuration. As the first known structures of a GT-36 enzyme, we determined the crystal structure of ChBP in a ternary complex with GlcNAc and SO4. It is also the first structures of an inverting phosphorolytic enzyme in a complex with a sugar and a sulfate ion, and reveals a pseudo-ternary complex structure of enzyme-sugar-phosphate. ChBP comprises a β sandwich domain and an (α/α)6 barrel domain, constituting a distinctive structure among GT families. Instead, it shows significant structural similarity with glycoside hydrolase (GH) enzymes, glucoamylases (GH-15), and maltose phosphorylase (GH-65) in clan GH-L. The structural similarity reported here, together with distant sequence similarities between ChBP and GHs, led to the reclassification of family GT-36 into a novel GH family, namely GH-94.

Original languageEnglish
Pages (from-to)937-947
Number of pages11
JournalStructure
Volume12
Issue number6
DOIs
Publication statusPublished - 2004 Jun
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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