Ontology highlight
ABSTRACT:
SUBMITTER: Arold ST
PROVIDER: S-EPMC2936596 | biostudies-literature | 2010 Sep
REPOSITORIES: biostudies-literature
Arold Stefan T ST Leonard Paul G PG Parkinson Gary N GN Ladbury John E JE
Proceedings of the National Academy of Sciences of the United States of America 20100823 36
The histone-like nucleoid structuring (H-NS) protein plays a fundamental role in DNA condensation and is a key regulator of enterobacterial gene expression in response to changes in osmolarity, pH, and temperature. The protein is capable of high-order self-association via interactions of its oligomerization domain. Using crystallography, we have solved the structure of this complete domain in an oligomerized state. The observed superhelical structure establishes a mechanism for the self-associat ...[more]