Analysis of the thermostability determinants of hyperthermophilic esterase EstE1 based on its predicted three-dimensional structure.
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.
Rhee
Jin-Kyu
JK
Department of Biotechnology, Yonsei University, 134 Shinchon-dong, Seodaemun-gu, Seoul 120-749, South Korea.
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
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
D004950:Esterases