File:Crystal-Structure-of-an-Ammonia-Permeable-Aquaporin-pbio.1002411.s008.ogv
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Original file (Ogg multiplexed audio/video file, Theora/Vorbis, length 38 s, 1,440 × 1,080 pixels, 1.11 Mbps overall, file size: 5.02 MB)
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[edit]DescriptionCrystal-Structure-of-an-Ammonia-Permeable-Aquaporin-pbio.1002411.s008.ogv |
English: MD simulation demonstrates spontaneous ammonia permeation. AtTIP2;1 monomer is displayed in side view with LCP-His 131 of the selectivity filter as well as Asn 83 and Asn 197 in the NPA region shown as sticks. An ammonia molecule (sphere representation) enters the main pore from the cytosolic side of the protein. During permeation of the pore, ammonia reorients such that its free electron pair points towards the asparagines at the protein center. In the course of the video, which corresponds to 2.94 ns, the imidazole group of LCP-His 131 can be observed rotating by 180° and back again. |
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Source | S1 Movie from Kirscht A, Kaptan S, Bienert G, Chaumont F, Nissen P, de Groot B, Kjellbom P, Gourdon P, Johanson U (2016). "Crystal Structure of an Ammonia-Permeable Aquaporin". PLOS Biology. DOI:10.1371/journal.pbio.1002411. PMID 27028365. PMC: 4814140. | ||
Author | Kirscht A, Kaptan S, Bienert G, Chaumont F, Nissen P, de Groot B, Kjellbom P, Gourdon P, Johanson U | ||
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This file is licensed under the Creative Commons Attribution 4.0 International license.
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Date/Time | Thumbnail | Dimensions | User | Comment | |
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current | 21:54, 18 October 2016 | 38 s, 1,440 × 1,080 (5.02 MB) | 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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Short title | MD simulation demonstrates spontaneous ammonia permeation. |
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Author | Kirscht A, Kaptan S, Bienert G, Chaumont F, Nissen P, de Groot B, Kjellbom P, Gourdon P, Johanson U |
Usage terms | http://creativecommons.org/licenses/by/4.0/ |
Image title | AtTIP2;1 monomer is displayed in side view with LCP-His 131 of the selectivity filter as well as Asn 83 and Asn 197 in the NPA region shown as sticks. An ammonia molecule (sphere representation) enters the main pore from the cytosolic side of the protein. During permeation of the pore, ammonia reorients such that its free electron pair points towards the asparagines at the protein center. In the course of the video, which corresponds to 2.94 ns, the imidazole group of LCP-His 131 can be observed rotating by 180° and back again. |
Software used | |
Date and time of digitizing | 2016-03-30 |