[HTML][HTML] Intra-and Intermonomer Interactions Are Required to Synergistically Facilitate ATP Hydrolysis in Hsp90*♦
CN Cunningham, KA Krukenberg, DA Agard - Journal of Biological …, 2008 - ASBMB
Nucleotide-dependent conformational changes of the constitutively dimeric molecular
chaperone Hsp90 are integral to its molecular mechanism. Recent full-length crystal
structures (Protein Data Bank codes 2IOQ, 2CG9, AND 2IOP) of Hsp90 homologs reveal
large scale quaternary domain rearrangements upon the addition of nucleotides. Although
previous work has shown the importance of C-terminal domain dimerization for efficient ATP
hydrolysis, which should imply cooperativity, other studies suggest that the two ATPases …
chaperone Hsp90 are integral to its molecular mechanism. Recent full-length crystal
structures (Protein Data Bank codes 2IOQ, 2CG9, AND 2IOP) of Hsp90 homologs reveal
large scale quaternary domain rearrangements upon the addition of nucleotides. Although
previous work has shown the importance of C-terminal domain dimerization for efficient ATP
hydrolysis, which should imply cooperativity, other studies suggest that the two ATPases …