Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties.

ABSTRACT:

Background

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.

Results

Here we report for the first time the 2.1-A resolution crystal structure of EstE1. The three-dimensional structure of EstE1 exhibits a classic alpha/beta hydrolase fold with a central parallel-stranded beta sheet surrounded by alpha helices on bo

SUBMITTER: Byun JS 

PROVIDER: S-EPMC1936996 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature