Figures
Structural transitions of the chaperonin GroEL during its allosteric cycle.
The bacterial chaperonin GroEL is an ATP-regulated molecular machine. It assists misfolded or partially folded proteins to unfold and refold into the correct native structure. The molecule consists of two rings, each composed of seven subunits. A dominant mechanism of motion during this process, which is predicted by the elastic network model, is the concerted counter-rotation of the two rings. This image displays four successive snapshots, viewed from the top, corresponding to successive steps of this allosteric process (see Yang et al., doi:10.1371/journal.pcbi.1000360).
Image Credit: The image was created by Zheng Yang (University of Pittsburgh, United States of America).
Citation: (2009) PLoS Computational Biology Issue Image | Vol. 5(4) April 2009. PLoS Comput Biol 5(4): ev05.i04. https://doi.org/10.1371/image.pcbi.v05.i04
Published: April 24, 2009
Copyright: © 2009 Yang et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
The bacterial chaperonin GroEL is an ATP-regulated molecular machine. It assists misfolded or partially folded proteins to unfold and refold into the correct native structure. The molecule consists of two rings, each composed of seven subunits. A dominant mechanism of motion during this process, which is predicted by the elastic network model, is the concerted counter-rotation of the two rings. This image displays four successive snapshots, viewed from the top, corresponding to successive steps of this allosteric process (see Yang et al., doi:10.1371/journal.pcbi.1000360).
Image Credit: The image was created by Zheng Yang (University of Pittsburgh, United States of America).