Ontology highlight
ABSTRACT:
SUBMITTER: Weaver CL
PROVIDER: S-EPMC5649362 | biostudies-literature | 2017 Apr
REPOSITORIES: biostudies-literature
Weaver Clarissa L CL Duran Elizabeth C EC Mack Korrie L KL Lin JiaBei J Jackrel Meredith E ME Sweeny Elizabeth A EA Shorter James J Lucius Aaron L AL
Biochemistry 20170410 15
Recent Hsp104 structural studies have reported both planar and helical models of the hexameric structure. The conformation of Hsp104 monomers within the hexamer is affected by nucleotide ligation. After nucleotide-driven hexamer formation, Hsp104-catalyzed disruption of protein aggregates requires binding to the peptide substrate. Here, we examine the oligomeric state of Hsp104 and its peptide binding competency in the absence of nucleotide and in the presence of ADP, ATPγS, AMPPNP, or AMPPCP. S ...[more]