Ontology highlight
ABSTRACT:
SUBMITTER: Santiago-Frangos A
PROVIDER: S-EPMC6561178 | biostudies-literature | 2019 May
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20190510 22
We have solved the X-ray crystal structure of the RNA chaperone protein Hfq from the alpha-proteobacterium <i>Caulobacter crescentus</i> to 2.15-Å resolution, resolving the conserved core of the protein and the entire C-terminal domain (CTD). The structure reveals that the CTD of neighboring hexamers pack in crystal contacts, and that the acidic residues at the C-terminal tip of the protein interact with positive residues on the rim of Hfq, as has been recently proposed for a mechanism of modula ...[more]