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Applied and Environmental Microbiology, April 2006, p. 3021-3025, Vol. 72, No. 4
0099-2240/06/$08.00+0 doi:10.1128/AEM.72.4.3021-3025.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
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Department of Biotechnology, Yonsei University, Seoul 120-749, South Korea,1 R&D Center, IDRTech Inc., Sungnam 463-480, South Korea,2 Department of Bioinformatics and Life Science and CAMDRC, Soongsil University, Seoul 156-743, South Korea,3 Department of Biology, Yonsei University, Seoul 120-749, South Korea,4 Korea Research Institute of Bioscience and Biotechnology, Taejon 305-600, South Korea5
Received 22 December 2005/ Accepted 6 February 2006
The three-dimensional (3D) structure of the hyperthermophilic esterase EstE1 was constructed by homology modeling using Archaeoglobus fulgidus esterase as a reference, and the thermostability-structure relationship was analyzed. Our results verified the predicted 3D structure of EstE1 and identified the ion pair networks and hydrophobic interactions that are critical determinants for the thermostability of EstE1.
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