File:Allosteric-Communication-in-Myosin-V-From-Small-Conformational-Changes-to-Large-Directed-Movements-pcbi.1000129.s002.ogv
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Size of this JPG preview of this OGG file: 800 × 471 pixels. Other resolutions: 320 × 188 pixels | 640 × 377 pixels | 1,060 × 624 pixels.
Original file (Ogg Theora video file, length 5.1 s, 1,060 × 624 pixels, 1.64 Mbps, file size: 1,023 KB)
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[edit]DescriptionAllosteric-Communication-in-Myosin-V-From-Small-Conformational-Changes-to-Large-Directed-Movements-pcbi.1000129.s002.ogv |
English: The NMSM rearrangement of the P-loop and switch I. The movie shows the rigor to post-rigor rearrangement of the P-loop and switch I nucleotide-binding elements as described by the optimal superposition of the 40 lowest-frequency rigor modes. The rigor (thick tube) and the post-rigor (thin tube) structures with the N-terminal subdomain aligned are shown in colors and grey, respectively. The ATP molecule in the post-rigor structure is shown in white as a stick representation. The color code is as follows: the N and U50 subdomains are colored in orange and blue; the P-loop, switch I, and switch II linkers are colored in cyan, magenta and yellow, respectively. The movie shows the way switch I approaches the P-loop and moves “over” it to coordinate the nucleotide. |
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Source | Video S2 from Cecchini M, Houdusse A, Karplus M (2008). "Allosteric Communication in Myosin V: From Small Conformational Changes to Large Directed Movements". PLOS Computational Biology. DOI:10.1371/journal.pcbi.1000129. PMID 18704171. PMC: 2497441. | ||
Author | Cecchini M, Houdusse A, Karplus M | ||
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Date/Time | Thumbnail | Dimensions | User | Comment | |
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current | 17:43, 16 November 2012 | 5.1 s, 1,060 × 624 (1,023 KB) | Open Access Media Importer Bot (talk | contribs) | Automatically uploaded media file from Open Access source. Please report problems or suggestions here. |
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Author | Cecchini M, Houdusse A, Karplus M |
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Usage terms | http://creativecommons.org/licenses/by/3.0/ |
Image title | The NMSM rearrangement of the P-loop and switch I. The movie shows the rigor to post-rigor rearrangement of the P-loop and switch I nucleotide-binding elements as described by the optimal superposition of the 40 lowest-frequency rigor modes. The rigor (thick tube) and the post-rigor (thin tube) structures with the N-terminal subdomain aligned are shown in colors and grey, respectively. The ATP molecule in the post-rigor structure is shown in white as a stick representation. The color code is as follows: the N and U50 subdomains are colored in orange and blue; the P-loop, switch I, and switch II linkers are colored in cyan, magenta and yellow, respectively. The movie shows the way switch I approaches the P-loop and moves ?over? it to coordinate the nucleotide. |
Software used | Xiph.Org libtheora 1.1 20090822 (Thusnelda) |
Date and time of digitizing | 2008-08 |