title: Analysis of the thermostability determinants of hyperthermophilic esterase EstE1 based on its predicted three-dimensional structure.
abstract: 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.
authors.affiliation: Department of Biotechnology, Yonsei University, 134 Shinchon-dong, Seodaemun-gu, Seoul 120-749, South Korea.
authors.forename: Jin-Kyu
authors.initials: JK
authors.lastname: Rhee
authors.forename: Do-Yun
authors.initials: DY
authors.lastname: Kim
authors.forename: Dae-Gyun
authors.initials: DG
authors.lastname: Ahn
authors.forename: Jung-Hyuk
authors.initials: JH
authors.lastname: Yun
authors.forename: Seung-Hwan
authors.initials: SH
authors.lastname: Jang
authors.forename: Hang-Cheol
authors.initials: HC
authors.lastname: Shin
authors.forename: Hyun-Soo
authors.initials: HS
authors.lastname: Cho
authors.forename: Jae-Gu
authors.initials: JG
authors.lastname: Pan
authors.forename: Jong-Won
authors.initials: JW
authors.lastname: Oh
mesh_terms: D019611:Archaeoglobus fulgidus / Q000201:enzymology*; D004795:Enzyme Stability; D004950:Esterases / Q000737:chemistry* / Q000378:metabolism*; D006358:Hot Temperature; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D013329:Structure-Activity Relationship
chemical_list: D004950:Esterases