6CL4

LipC12 - Lipase from metagenomics

Summary for 6CL4

• Entry DOI: 10.2210/pdb6cl4/pdb
• Descriptor: Lipase C12 (2 entities in total)
• Functional Keywords: lipase, hydrolase
• Biological source: uncultured bacterium
• Total number of polymer chains: 1
• Total formula weight: 33433.78

Authors

Iulek, J.,Martini, V.P.,Krieger, N.,Glogauer, A.,Souza, E.M. (deposition date: 2018-03-01, release date: 2019-03-13, Last modification date: 2023-10-04)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.64 Å)