Preparation and preliminary X-ray analysis of the catalytic module of β-1,3-xylanase from the marine bacterium Vibrio sp. AX-4

Keishi Sakaguchi, Masashi Kiyohara, Nobuhisa Watanabe, Kuniko Yamaguchi, Makoto Ito, Takashi Kawamura, Isao Tanaka

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

β-1,3-xylanase (1,3-β-D-xylan xylanohydrolase; EC 3.2.1.32) is an enzyme capable of hydrolyzing β-1,3-xylan. The newly cloned β-1,3-xylanase from the marine bacterium Vibrio sp. AX-4 (XYL4) exhibited a modular structure consisting of three modules: an N-terminal catalytic module belonging to glycoside hydrolase family 26 and two C-terminal xylan-binding modules belonging to carbohydrate-binding module family 31. Despite substantial crystallization screening, crystallization of the recombinant XYL4 was not accomplished. However, the deletion mutant of XYL4, composed of a catalytic module without a xylan-binding module, was crystallized. The crystal belonged to space group P212121, with unit-cell parameters a = 51.6, b = 75.8, c = 82.0 Å. X-ray diffraction data were collected to 1.44 Å resolution.

Original languageEnglish
Pages (from-to)1470-1472
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume60
Issue number8
DOIs
Publication statusPublished - Aug 1 2004

All Science Journal Classification (ASJC) codes

  • Structural Biology

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