Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX-Reference-Cited by-同舟云学术

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Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX

Published:2015-04-13 Issue:5 Volume:22 Page:411-416
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Stinson Benjamin M,Baytshtok Vladimir,Schmitz Karl R,Baker Tania A,Sauer Robert T

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.3012.pdf

Reference28 articles.

1. Baker, T.A. & Sauer, R.T. ClpXP, an ATP-powered unfolding and protein-degradation machine. Biochim. Biophys. Acta 1823, 15–28 (2012).

2. Hersch, G.L., Burton, R.E., Bolon, D.N., Baker, T.A. & Sauer, R.T. Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine. Cell 121, 1017–1027 (2005).

3. Stinson, B.M. et al. Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine. Cell 153, 628–639 (2013).

4. Glynn, S.E., Martin, A., Nager, A.R., Baker, T.A. & Sauer, R.T. Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine. Cell 139, 744–756 (2009).

5. Smith, D.M., Fraga, H., Reis, C., Kafri, G. & Goldberg, A.L. ATP binds to proteasomal ATPases in pairs with distinct functional effects, implying an ordered reaction cycle. Cell 144, 526–538 (2011).

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