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 language | English |
|---|---|
| Pages (from-to) | 238-244 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 412 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2011 Aug 26 |
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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 journal › Article
}
TY - JOUR
T1 - Crystal structure of a key enzyme in the agarolytic pathway, α-neoagarobiose hydrolase from Saccharophagus degradans 2-40
AU - Ha, Sung Chul
AU - Lee, Saeyoung
AU - Lee, Jonas
AU - Kim, Hee Taek
AU - Ko, Hyeok Jin
AU - Kim, Kyoung Heon
AU - Choi, In-Geol
PY - 2011/8/26
Y1 - 2011/8/26
N2 - 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.
AB - 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.
KW - α-Neoagarobiose hydrolase
KW - Agarolytic pathway
KW - Five-bladed β-propeller fold
KW - Glycoside hydrolase family 117
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UR - http://www.scopus.com/inward/citedby.url?scp=80052038763&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2011.07.073
DO - 10.1016/j.bbrc.2011.07.073
M3 - Article
VL - 412
SP - 238
EP - 244
JO - The BMJ
JF - The BMJ
SN - 0730-6512
IS - 2
ER -