Analysis of the thermostability determinants of hyperthermophilic esterase EstE1 based on its predicted three-dimensional structure.
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ABSTRACT:
SUBMITTER: Rhee JK
PROVIDER: S-EPMC1449032 | biostudies-literature | 2006 Apr
REPOSITORIES: biostudies-literature
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Analysis of the thermostability determinants of hyperthermophilic esterase EstE1 based on its predicted three-dimensional structure.
Rhee Jin-Kyu JK Kim Do-Yun DY Ahn Dae-Gyun DG Yun Jung-Hyuk JH Jang Seung-Hwan SH Shin Hang-Cheol HC Cho Hyun-Soo HS Pan Jae-Gu JG Oh Jong-Won JW
Applied and environmental microbiology 20060401 4
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. ...[more]
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