2C7B

The Crystal Structure of EstE1, a New Thermophilic and Thermostable Carboxylesterase Cloned from a Metagenomic Library

Summary for 2C7B

• Entry DOI: 10.2210/pdb2c7b/pdb
• Related: 2BZQ
• Descriptor: CARBOXYLESTERASE (2 entities in total)
• Functional Keywords: carboxyesterase, thermophilic enzyme, hydrolase, hsl, alpha/beta hydrolase fold
• Biological source: UNCULTURED ARCHAEON
• Total number of polymer chains: 2
• Total formula weight: 68116.33

Authors

Byun, J.-S.,Rhee, J.-K.,Kim, D.-U.,Oh, J.-W.,Cho, H.-S. (deposition date: 2005-11-21, release date: 2005-12-01, Last modification date: 2011-07-13)

Primary citation

Byun, J.-S.,Rhee, J.-K.,Kim, N.D.,Yoon, J.,Kim, D.-U.,Koh, E.,Oh, J.-W.,Cho, H.-S.
Crystal Structure of Hyperthermophilic Esterase Este1 and the Relationship between its Dimerization and Thermostability Properties.
Bmc Struct.Biol., 7:47-, 2007

PubMed Abstract: 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.

PubMed: 17625021
DOI: 10.1186/1472-6807-7-47

Experimental method

X-RAY DIFFRACTION (2.3 Å)