Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125

Shinya Fushinobu, Masafumi Hidaka, Yuji Honda, Takayoshi Wakagi, Hirofumi Shoun, Motomitsu Kitaoka

Research output: Contribution to journalArticlepeer-review

49 Citations (Scopus)

Abstract

Reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125 (Rex) hydrolyzes xylooligosaccharides whose degree of polymerization is greater than or equal to 3, releasing the xylose unit at the reducing end. It is a unique exo-type glycoside hydrolase that recognizes the xylose unit at the reducing end in a very strict manner, even discriminating the β-anomeric hydroxyl configuration from the α-anomer or 1-deoxyxylose. We have determined the crystal structures of Rex in unliganded and complex forms at 1.35-2.20-Å resolution and revealed the structural aspects of its three subsites ranging from -2 to +1. The structure of Rex was compared with those of endo-type enzymes in glycoside hydrolase subfamily 8a (GH-8a). The catalytic machinery of Rex is basically conserved with other GH-8a enzymes. However, subsite +2 is blocked by a barrier formed by a kink in the loop before helix α10. His-319 in this loop forms a direct hydrogen bond with the β-hydroxyl of xylose at subsite +1, contributing to the specific recognition of anomers at the reducing end.

Original languageEnglish
Pages (from-to)17180-17186
Number of pages7
JournalJournal of Biological Chemistry
Volume280
Issue number17
DOIs
Publication statusPublished - 2005 Apr 29

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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