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

doi:10.1016/j.bbrc.2011.07.073

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 journal › Article › peer-review

79 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 language	English
Pages (from-to)	238-244
Number of pages	7
Journal	Biochemical and biophysical research communications
Volume	412
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2011.07.073
Publication status	Published - 2011 Aug 26

Bibliographical note

Funding Information:
We thank to Prof. Sung-Hou Kim of University of California, Berkeley, Prof. Kwang Yeon Hwang and Joseph Song of Korea University. This work is supported by the National Research Foundation (NRF) Grant funded by the Korea government (MEST) (Nos. 2009-0068606 and 2011-0015629 ).

Keywords

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

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2011.07.073

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

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. {\AA}, 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.",

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author = "Ha, {Sung Chul} and Saeyoung Lee and Jonas Lee and Kim, {Hee Taek} and Ko, {Hyeok Jin} and Kim, {Kyoung Heon} and Choi, {In Geol}",

note = "Funding Information: We thank to Prof. Sung-Hou Kim of University of California, Berkeley, Prof. Kwang Yeon Hwang and Joseph Song of Korea University. This work is supported by the National Research Foundation (NRF) Grant funded by the Korea government (MEST) (Nos. 2009-0068606 and 2011-0015629 ). ",

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AU - Lee, Jonas

AU - Kim, Hee Taek

AU - Ko, Hyeok Jin

AU - Kim, Kyoung Heon

AU - Choi, In Geol

N1 - Funding Information: We thank to Prof. Sung-Hou Kim of University of California, Berkeley, Prof. Kwang Yeon Hwang and Joseph Song of Korea University. This work is supported by the National Research Foundation (NRF) Grant funded by the Korea government (MEST) (Nos. 2009-0068606 and 2011-0015629 ).

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.

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KW - Five-bladed β-propeller fold

KW - Glycoside hydrolase family 117

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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