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Published August 26, 2011 | Supplemental Material
Journal Article Open

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

Abstract

In agarolytic microorganisms, a-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.

Additional Information

© 2011 Elsevier Inc. Received 17 July 2011. Available online 23 July 2011. 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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