Ontology highlight
ABSTRACT:
SUBMITTER: van den Worm SH
PROVIDER: S-EPMC147404 | biostudies-other | 1998 Mar
REPOSITORIES: biostudies-other
van den Worm S H SH Stonehouse N J NJ Valegârd K K Murray J B JB Walton C C Fridborg K K Stockley P G PG Liljas L L
Nucleic acids research 19980301 5
In MS2 assembly of phage particles results from an interaction between a coat protein dimer and a stem-loop of the RNA genome (the operator hairpin). Amino acid residues Thr45, which is universally conserved among the small RNA phages, and Thr59 are part of the specific RNA binding pocket and interact directly with the RNA; the former through a hydrogen bond, the latter through hydrophobic contacts. The crystal structures of MS2 protein capsids formed by mutants Thr45Ala and Thr59Ser, both with ...[more]