Crystallization and preliminary X-ray analysis of neoagarobiose hydrolase from Saccharophagus degradans 2-40

Saeyoung Lee, Jonas Yun Lee, Sung Chul Ha, Jina Jung, Dong Hae Shin, Kyoung Heon Kim, In Geol Choi

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

Many agarolytic bacteria degrade agar polysaccharide into the disaccharide unit neoagarobiose [O-3,6-anhydro -α L-galactopyranosyl-(1→3)-D- galactose] using various β-agarases. Neoagarobiose hydrolase is an enzyme that acts on the α- 1,3 linkage in neoagarobiose to yield D-galactose and 3,6-anhydro-L-galactose. This activity is essential in both the metabolism of agar by agarolytic bacteria and the production of fermentable sugars from agar biomass for bioenergy production. Neoagarobiose hydrolase from the marine bacterium Saccharophagus degradans 2-40 was overexpressed in Escherichia coli and crystallized in the monoclinic space group C2, with unit-cell parameters a = 129.83, b = 76.81, c = 90.11 Å, β = 101.86°. The crystals diffracted to 1.98 Å resolution and possibly contains two molecules in the asymmetric unit.

Original languageEnglish
Pages (from-to)1299-1301
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume65
Issue number12
DOIs
Publication statusPublished - 2009

Keywords

  • Bioenergy
  • Hydrolases
  • Neoagarobiose

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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