Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 114, Issue 23, Pages 6040-6045Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1619843114
Keywords
laser trapping; parallel pathways; elasticity; force; protein extension
Categories
Funding
- Deutsche Forschungsgemeinschaft [SFB 1035/A5, ZO 291/1-1]
- National Science Foundation [MCB-1412183]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1412183] Funding Source: National Science Foundation
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Owing to the cooperativity of protein structures, it is often almost impossible to identify independent subunits, flexible regions, or hinges simply by visual inspection of static snapshots. Here, we use single-molecule force experiments and simulations to apply tension across the substrate binding domain (SBD) of heat shock protein 70 (Hsp70) to pinpoint mechanical units and flexible hinges. The SBD consists of two nanomechanical units matching 3D structural parts, called the alpha- and beta-subdomain. We identified a flexible region within the rigid beta-subdomain that gives way under load, thus opening up the alpha/beta interface. In exactly this region, structural changes occur in the ATP-induced opening of Hsp70 to allow substrate exchange. Our results show that the SBD's ability to undergo large conformational changes is already encoded by passive mechanics of the individual elements.
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