The Structure of ClpB: A Molecular Chaperone that Rescues Proteins from an Aggregated State
Sukyeong Lee,Mathew E. Sowa,Yo-hei Watanabe,Paul B. Sigler,Wah Chiu,Masasuke Yoshida,Francis T.F. Tsai +6 more
TLDR
Taking together, mutagenesis and biochemical data show that both the relative position and motion of this coiled coil are critical for chaperone function, and propose a mechanism by which an ATP-driven conformational change is coupled to a large coiled-coil motion, which is indispensable for protein disaggregation.About:
This article is published in Cell.The article was published on 2003-10-17 and is currently open access. It has received 433 citations till now. The article focuses on the topics: CLPB & Chaperone (protein).read more
Citations
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Recombinant protein folding and misfolding in Escherichia coli.
François Baneyx,Mirna Mujacic +1 more
TL;DR: The past 20 years have seen enormous progress in the understanding of the mechanisms used by the enteric bacterium Escherichia coli to promote protein folding, support protein translocation and handle protein misfolding, and these insights have been exploited to tackle the problems of inclusion body formation, proteolytic degradation and disulfide bond generation.
Journal ArticleDOI
AAA+ proteins: have engine, will work.
TL;DR: The structural organization of AAA+ proteins, the conformational changes they undergo, the range of different reactions they catalyse, and the diseases associated with their dysfunction are reviewed.
Journal ArticleDOI
Targeting apoptosis in cancer therapy
TL;DR: The main pathways that regulate apoptosis as well as other signalling pathways that interact with them are presented, highlighting actionable molecular targets for anticancer therapy and an overview of therapeutic agents exploiting apoptosis currently in clinical translation and known mechanisms of resistance to these agents are provided.
Journal ArticleDOI
Chaperone machines for protein folding, unfolding and disaggregation
TL;DR: The structural basis of their mechanism of action is being unravelled and typically involves massive displacements of 20–30 kDa domains over distances of 20-50 Å and rotations of up to 100°.
Journal ArticleDOI
AAA+ proteases: ATP-fueled machines of protein destruction.
Robert T. Sauer,Tania A. Baker +1 more
TL;DR: The current understanding of the molecular mechanisms of substrate recognition, adaptor function, and ATP-fueled unfolding and translocation are reviewed.
References
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Improved methods for building protein models in electron density maps and the location of errors in these models.
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Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold.
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