5AOC

The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-valerate bound

5AOC の概要

• エントリーDOI: 10.2210/pdb5aoc/pdb
• 関連するPDBエントリー: 5AO9 5AOA 5AOB
• 分子名称: ESTERASE, PENTANOIC ACID, TETRAETHYLENE GLYCOL, ... (7 entities in total)
• 機能のキーワード: hydrolase, carboxyl, carboxyl esterase
• 由来する生物種: THERMOGUTTA TERRIFONTIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32836.78

構造登録者

Sayer, C.,Szabo, Z.,Isupov, M.N.,Ingham, C.,Littlechild, J.A. (登録日: 2015-09-10, 公開日: 2015-12-09, 最終更新日: 2024-01-10)

主引用文献

Sayer, C.,Szabo, Z.,Isupov, M.N.,Ingham, C.,Littlechild, J.A.
The Structure of a Novel Thermophilic Esterase from the Planctomycetes Species, Thermogutta Terrifontis Reveals an Open Active Site due to a Minimal 'CAP' Domain.
Front.Microbiol., 6:1294-, 2015

PubMed Abstract: A carboxyl esterase (TtEst2) has been identified in a novel thermophilic bacterium, Thermogutta terrifontis from the phylum Planctomycetes and has been cloned and over-expressed in Escherichia coli. The enzyme has been characterized biochemically and shown to have activity toward small p-nitrophenyl (pNP) carboxylic esters with optimal activity for pNP-acetate. The enzyme shows moderate thermostability retaining 75% activity after incubation for 30 min at 70°C. The crystal structures have been determined for the native TtEst2 and its complexes with the carboxylic acid products propionate, butyrate, and valerate. TtEst2 differs from most enzymes of the α/β-hydrolase family 3 as it lacks the majority of the 'cap' domain and its active site cavity is exposed to the solvent. The bound ligands have allowed the identification of the carboxyl pocket in the enzyme active site. Comparison of TtEst2 with structurally related enzymes has given insight into how differences in their substrate preference can be rationalized based upon the properties of their active site pockets.

PubMed: 26635762
DOI: 10.3389/FMICB.2015.01294

実験手法

X-RAY DIFFRACTION (1.79 Å)