ArticleActa crystallographica. Section D, Biological crystallography2014
Elements in nucleotide sensing and hydrolysis of the AAA+ disaggregation machine ClpB: a structure-based mechanistic dissection of a molecular motor.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 21 citations in OpenAlex.
- Mechanism of cooperative strigolactone perception by the MAX2 ubiquitin ligase-receptor-substrate complex.Nature communications · 2025Article
- Modular and coordinated activity of AAA+ active sites in the double-ring ClpA unfoldase of the ClpAP protease.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Significance of Individual Domains of ClpL: A Novel Chaperone fromBiochemistry · 2020Article
- Genome-wide analysis of the HSP101/CLPB gene family for heat tolerance in hexaploid wheat.Scientific reports · 2020Article
- A History of Molecular Chaperone Structures in the Protein Data Bank.International journal of molecular sciences · 2019Review
- Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 Structures.Biochemistry · 2017Article
- Mutant Analysis Reveals Allosteric Regulation of ClpB Disaggregase.Frontiers in molecular biosciences · 2017Article
- Structural Elements Regulating AAA+ Protein Quality Control Machines.Frontiers in molecular biosciences · 2017Review
- Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions.Frontiers in molecular biosciences · 2017Review
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- Bi-allelic CLPB mutations cause cataract, renal cysts, nephrocalcinosis and 3-methylglutaconic aciduria, a novel disorder of mitochondrial protein disaggregation.Journal of inherited metabolic disease · 2015Article
- trans-Acting arginine residues in the AAA+ chaperone ClpB allosterically regulate the activity through inter- and intradomain communication.The Journal of biological chemistry · 2014Article
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
ATPases of the AAA+ superfamily are large oligomeric molecular machines that remodel their substrates by converting the energy from ATP hydrolysis into mechanical force. This study focuses on the molecular chaperone ClpB, the bacterial homologue of Hsp104, which reactivates aggregated proteins under cellular stress conditions. Based on high-resolution crystal structures in different nucleotide states, mutational analysis and nucleotide-binding kinetics experiments, the ATPase cycle of the C-terminal nucleotide-binding domain (NBD2), one of the motor subunits of this AAA+ disaggregation machine, is dissected mechanistically. The results provide insights into nucleotide sensing, explaining how the conserved sensor 2 motif contributes to the discrimination between ADP and ATP binding. Furthermore, the role of a conserved active-site arginine (Arg621), which controls binding of the essential Mg2+ ion, is described. Finally, a hypothesis is presented as to how the ATPase activity is regulated by a conformational switch that involves the essential Walker A lysine. In the proposed model, an unusual side-chain conformation of this highly conserved residue stabilizes a catalytically inactive state, thereby avoiding unnecessary ATP hydrolysis.
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