Ha, Sung Chul and Lee, Saeyoung and Lee, Jonas and Kim, Hee Taek and Ko, Hyeok-Jin and Kim, Kyoung Heon and Choi, In-Geol (2011) Crystal structure of a key enzyme in the agarolytic pathway, α-neoagarobiose hydrolase from Saccharophagus degradans 2–40. Biochemical and Biophysical Research Communications, 412 (2). pp. 238-244. ISSN 0006-291X http://resolver.caltech.edu/CaltechAUTHORS:20110930-074157090
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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).|
|Subject Keywords:||α-Neoagarobiose hydrolase Five-bladed b-propeller fold Agarolytic pathway Glycoside hydrolase family 117|
|Official Citation:||Sung Chul Ha, Saeyoung Lee, Jonas Lee, Hee Taek Kim, Hyeok-Jin Ko, Kyoung Heon Kim, In-Geol Choi, Crystal structure of a key enzyme in the agarolytic pathway, α-neoagarobiose hydrolase from Saccharophagus degradans 2–40, Biochemical and Biophysical Research Communications, Volume 412, Issue 2, 26 August 2011, Pages 238-244, ISSN 0006-291X, 10.1016/j.bbrc.2011.07.073. (http://www.sciencedirect.com/science/article/pii/S0006291X1101299X)|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Ruth Sustaita|
|Deposited On:||30 Sep 2011 16:55|
|Last Modified:||30 Sep 2011 16:55|
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