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PDBsum entry 2d9d
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References listed in PDB file
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Key reference
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Title
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The c-Terminal bag domain of bag5 induces conformational changes of the hsp70 nucleotide-Binding domain for ADP-Atp exchange.
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Authors
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A.Arakawa,
N.Handa,
N.Ohsawa,
M.Shida,
T.Kigawa,
F.Hayashi,
M.Shirouzu,
S.Yokoyama.
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Ref.
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Structure, 2010,
18,
309-319.
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PubMed id
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Abstract
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ADP-ATP exchange by the molecular chaperone Hsp70 is enhanced by several
cochaperones. BAG5 consists of five BAG domains and associates with the
nucleotide-binding domain (NBD) of Hsp70. The overexpression of BAG5 in the
cytosol reportedly disturbs Hsp70-mediated protein refolding and induces
Parkinson's disease. In the present study, we found that the fifth BAG domain
(BD5) of BAG5 is responsible for the interaction between Hsp70 and BAG5. We also
determined the crystal structures of the BD5*NBD complex. BD5 binding caused two
different types of NBD conformational changes, which both disrupted the
nucleotide-binding groove. In fact, BD5 reduced the affinity of the NBD for ADP.
Moreover, BD5, as well as the full-length BAG5, accelerated Hsp70-mediated
refolding in an in vitro assay. Therefore, BAG5 can function as the nucleotide
exchange factor of Hsp70 for the enhancement of protein refolding.
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