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Article

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

BMC structural biology - 12 Jul 2007

Byun Jung-Sue, Rhee Jin-Kyu, Kim Nam Doo, Yoon Jeonghyeok, Kim Dong-Uk, Koh Eunhee, Oh Jong-Won, Cho Hyun-Soo

Abstract excerpt

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...

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Identifiers

PMID: 17625021
DOI: 10.1186/1472-6807-7-47
PMCID: PMC1936996

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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