Unknown

Dataset Information

0

Crystal structure of Proteus mirabilis lipase, a novel lipase from the Proteus/psychrophilic subfamily of lipase family I.1.


ABSTRACT: Bacterial lipases from family I.1 and I.2 catalyze the hydrolysis of triacylglycerol between 25-45°C and are used extensively as biocatalysts. The lipase from Proteus mirabilis belongs to the Proteus/psychrophilic subfamily of lipase family I.1 and is a promising catalyst for biodiesel production because it can tolerate high amounts of water in the reaction. Here we present the crystal structure of the Proteus mirabilis lipase, a member of the Proteus/psychrophilic subfamily of I.1lipases. The structure of the Proteus mirabilis lipase was solved in the absence and presence of a bound phosphonate inhibitor. Unexpectedly, both the apo and inhibitor bound forms of P. mirabilis lipase were found to be in a closed conformation. The structure reveals a unique oxyanion hole and a wide active site that is solvent accessible even in the closed conformation. A distinct mechanism for Ca²? coordination may explain how these lipases can fold without specific chaperones.

SUBMITTER: Korman TP 

PROVIDER: S-EPMC3530535 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature

altmetric image

Publications

Crystal structure of Proteus mirabilis lipase, a novel lipase from the Proteus/psychrophilic subfamily of lipase family I.1.

Korman Tyler P TP   Bowie James U JU  

PloS one 20121226 12


Bacterial lipases from family I.1 and I.2 catalyze the hydrolysis of triacylglycerol between 25-45°C and are used extensively as biocatalysts. The lipase from Proteus mirabilis belongs to the Proteus/psychrophilic subfamily of lipase family I.1 and is a promising catalyst for biodiesel production because it can tolerate high amounts of water in the reaction. Here we present the crystal structure of the Proteus mirabilis lipase, a member of the Proteus/psychrophilic subfamily of I.1lipases. The s  ...[more]

Similar Datasets

2015-04-13 | GSE63321 | GEO
2015-04-13 | E-GEOD-63321 | biostudies-arrayexpress
2018-08-10 | GSE96042 | GEO
| S-EPMC8539402 | biostudies-literature
| S-EPMC2876570 | biostudies-literature
2010-06-07 | GSE17957 | GEO
| S-EPMC4094090 | biostudies-literature
| S-EPMC4638163 | biostudies-literature
| S-EPMC3133265 | biostudies-literature
| S-EPMC2258889 | biostudies-literature