File:Pathways-of-allosteric-regulation-in-Hsp70-chaperones-ncomms9308-s4.ogv
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[edit]DescriptionPathways-of-allosteric-regulation-in-Hsp70-chaperones-ncomms9308-s4.ogv |
English: Supplementary Movie 3 Supplementary Movie 3 (related to Fig. 5): ATP induced dynamics of the NBD. The movie shows a morph starting from an homology model of E. coli DnaK onto the structure of bovine Hsc70 in complex with ADP and phosphate (PDB ID 1HPM) to the ATP bound open conformation of DnaK (PDB ID 4B9Q) and back. Surface representation with lobe I in dark gray, lobe II in light gray, and residues interacting with SBDβ colored according effects on basal ATPase rate upon replacement with alanine (Y145A, F146A, D148A, R151A, K155A, R167A) or upon replacement of interacting residues (I168[D481A], D326[K414I]). Increase in basal ATPase rate less than 5-fold (yellow). 5 to 10-fold (orange), 11 to 15-fold (red), 16 to 20-fold (dark red), more than 26 to 84-fold (magenta). Morph was created on The Yale Morph Server (http://molmovdb.org/morph/) and visualized in PyMOL (The PyMOL Molecular Graphics System, Version 1.7.4 Schrödinger, LLC). |
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Source | Video file from Kityk R, Vogel M, Schlecht R, Bukau B, Mayer M (2015). "Pathways of allosteric regulation in Hsp70 chaperones". Nature Communications. DOI:10.1038/ncomms9308. PMID 26383706. PMC: 4595643. | ||
Author | Kityk R, Vogel M, Schlecht R, Bukau B, Mayer M | ||
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This file is licensed under the Creative Commons Attribution 4.0 International license.
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Short title | Supplementary Movie 3 |
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Author | Kityk R, Vogel M, Schlecht R, Bukau B, Mayer M |
Usage terms | http://creativecommons.org/licenses/by/4.0/ |
Image title | Supplementary Movie 3 (related to Fig. 5): ATP induced dynamics of the NBD. The movie shows a morph starting from an homology model of E. coli DnaK onto the structure of bovine Hsc70 in complex with ADP and phosphate (PDB ID 1HPM) to the ATP bound open conformation of DnaK (PDB ID 4B9Q) and back. Surface representation with lobe I in dark gray, lobe II in light gray, and residues interacting with SBDβ colored according effects on basal ATPase rate upon replacement with alanine (Y145A, F146A, D148A, R151A, K155A, R167A) or upon replacement of interacting residues (I168[D481A], D326[K414I]). Increase in basal ATPase rate less than 5-fold (yellow). 5 to 10-fold (orange), 11 to 15-fold (red), 16 to 20-fold (dark red), more than 26 to 84-fold (magenta). Morph was created on The Yale Morph Server (http://molmovdb.org/morph/) and visualized in PyMOL (The PyMOL Molecular Graphics System, Version 1.7.4 Schrödinger, LLC). |
Software used | Xiph.Org libtheora 1.1 20090822 (Thusnelda) |
Date and time of digitizing | 2015-09-18 |