2C7B

The Crystal Structure of EstE1, a New Thermophilic and Thermostable Carboxylesterase Cloned from a Metagenomic Library

2C7B の概要

• エントリーDOI: 10.2210/pdb2c7b/pdb
• 関連するPDBエントリー: 2BZQ
• 分子名称: CARBOXYLESTERASE (2 entities in total)
• 機能のキーワード: carboxyesterase, thermophilic enzyme, hydrolase, hsl, alpha/beta hydrolase fold
• 由来する生物種: UNCULTURED ARCHAEON
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68116.33

構造登録者

Byun, J.-S.,Rhee, J.-K.,Kim, D.-U.,Oh, J.-W.,Cho, H.-S. (登録日: 2005-11-21, 公開日: 2005-12-01, 最終更新日: 2024-11-20)

主引用文献

Byun, J.-S.,Rhee, J.-K.,Kim, N.D.,Yoon, J.,Kim, D.-U.,Koh, E.,Oh, J.-W.,Cho, H.-S.
Crystal Structure of Hyperthermophilic Esterase Este1 and the Relationship between its Dimerization and Thermostability Properties.
Bmc Struct.Biol., 7:47-, 2007

PubMed Abstract: EstE1 is a hyperthermophilic esterase belonging to the hormone-sensitive lipase family and was originally isolated by functional screening of a metagenomic library constructed from a thermal environmental sample. Dimers and oligomers may have been evolutionally selected in thermophiles because intersubunit interactions can confer thermostability on the proteins. The molecular mechanisms of thermostabilization of this extremely thermostable esterase are not well understood due to the lack of structural information.

PubMed: 17625021
DOI: 10.1186/1472-6807-7-47

実験手法

X-RAY DIFFRACTION (2.3 Å)