6CL4

LipC12 - Lipase from metagenomics

6CL4 の概要

• エントリーDOI: 10.2210/pdb6cl4/pdb
• 分子名称: Lipase C12 (2 entities in total)
• 機能のキーワード: lipase, hydrolase
• 由来する生物種: uncultured bacterium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33433.78

構造登録者

Iulek, J.,Martini, V.P.,Krieger, N.,Glogauer, A.,Souza, E.M. (登録日: 2018-03-01, 公開日: 2019-03-13, 最終更新日: 2023-10-04)

主引用文献

Martini, V.P.,Krieger, N.,Glogauer, A.,Souza, E.M.,Iulek, J.
Structure solution and analyses of the first true lipase obtained from metagenomics indicate potential for increased thermostability.
N Biotechnol, 53:65-72, 2019

PubMed Abstract: Metagenomics is a modern approach to discovery of new enzymes with novel properties. This article reports the structure of a new lipase, belonging to family I.1, obtained by means of metagenomics. Its structure presents a fold typical of α/β hydrolases, with the lid in closed conformation. The protein was previously shown to present high thermostability and to be stable in aqueous solutions of polar organic solvents at high concentrations [30% (V/V)]. Molecular dynamics studies showed that the protein maintains its structure well in organic solvents. They also suggested that its thermostability might be enhanced if it were mutated to present a disulfide bond similar to that typically found in lipase family I.2. These findings identify this lipase as a good candidate for further improvement through protein engineering.

PubMed: 31306784
DOI: 10.1016/j.nbt.2019.07.001

実験手法

X-RAY DIFFRACTION (2.64 Å)