Crystal structure of a key enzyme in the agarolytic pathway, α-neoagarobiose hydrolase from Saccharophagus degradans 2-40

Sung Chul Ha, Saeyoung Lee, Jonas Lee, Hee Taek Kim, Hyeok Jin Ko, Kyoung Heon Kim, In-Geol Choi

Research output: Contribution to journalArticle

49 Citations (Scopus)

Abstract

In agarolytic microorganisms, α-neoagarobiose hydrolase (NABH) is an essential enzyme to metabolize agar because it converts α-neoagarobiose (O-3,6-anhydro-alpha-l-galactopyranosyl-(1,3)-d-galactose) into fermentable monosaccharides (d-galactose and 3,6-anhydro-l-galactose) in the agarolytic pathway. NABH can be divided into two biological classes by its cellular location. Here, we describe a structure and function of cytosolic NABH from Saccharophagus degradans 2-40 in a native protein and d-galactose complex determined at 2.0 and 1.55. Å, respectively. The overall fold is organized in an N-terminal helical extension and a C-terminal five-bladed β-propeller catalytic domain. The structure of the enzyme-ligand (d-galactose) complex predicts a +1 subsite in the substrate binding pocket. The structural features may provide insights for the evolution and classification of NABH in agarolytic pathways.

Original languageEnglish
Pages (from-to)238-244
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume412
Issue number2
DOIs
Publication statusPublished - 2011 Aug 26

Fingerprint

Galactose
Crystal structure
Enzymes
Monosaccharides
Propellers
Microorganisms
Agar
Catalytic Domain
neoagarobiose hydrolase
Ligands
Substrates
Proteins

Keywords

  • α-Neoagarobiose hydrolase
  • Agarolytic pathway
  • Five-bladed β-propeller fold
  • Glycoside hydrolase family 117

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

Crystal structure of a key enzyme in the agarolytic pathway, α-neoagarobiose hydrolase from Saccharophagus degradans 2-40. / Ha, Sung Chul; Lee, Saeyoung; Lee, Jonas; Kim, Hee Taek; Ko, Hyeok Jin; Kim, Kyoung Heon; Choi, In-Geol.

In: Biochemical and Biophysical Research Communications, Vol. 412, No. 2, 26.08.2011, p. 238-244.

Research output: Contribution to journalArticle

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