ArticleCellular and molecular bioengineering2013
Nucleotide-dependent control of internal strains in ring-shaped AAA+ motors.
Article in Cellular and molecular bioengineering, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Structural basis for power stroke vs. Brownian ratchet mechanisms of motor proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Molecular dynamics simulations of nucleotide release from the circadian clock protein KaiC reveal atomic-resolution functional insights.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Probing Small Molecule Binding to Unfolded Polyprotein Based on its Elasticity and Refolding.Biophysical journal · 2016Article
- Marching to the beat of the ring: polypeptide translocation by AAA+ proteases.Trends in biochemical sciences · 2014Review
- Functions and mechanics of dynein motor proteins.Nature reviews. Molecular cell biology · 2013Review
- The ClpXP protease unfolds substrates using a constant rate of pulling but different gears.Cell · 2013Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The AAA+ (ATPase Associated with various cellular Activities) machinery represents an extremely successful and widely used design plan for biological motors. Recently found crystal structures are beginning to reveal nucleotide-dependent conformational changes in the canonical hexameric rings of the AAA+ motors. However, the physical mechanism by which ATP binding on one subunit allosterically propagates across the entire ring remains to be found. Here we analyze and compare structural organization of three ring-shaped AAA+ motors, ClpX, HslU, and dynein. By constructing multimers using subunits of identical conformations, we find that individual subunits locally possess helical geometries with varying pitch, radius, chirality, and symmetry number. These results suggest that binding of an ATP to a subunit imposes conformational constraint that must be accommodated by more flexible nucleotide-free subunits to relieve mechanical strain on the ring. Local deformation of the ring contour and subsequent propagation of strains may be a general strategy that AAA+ motors adopt to generate force while achieving functional diversity.
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Registered trials
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