File:Breakage-Reunion-Domain-of-Streptococcus-pneumoniae-Topoisomerase-IV-Crystal-Structure-of-a-Gram-pone.0000301.s003.ogv

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Breakage-Reunion-Domain-of-Streptococcus-pneumoniae-Topoisomerase-IV-Crystal-Structure-of-a-Gram-pone.0000301.s003.ogv (Ogg Theora video file, length 0.0 s, 682 × 480 pixels, 0 bps, file size: 8.75 MB)

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English: A schematic process of DNA binding and recognition by S. pneumoniae ParC. The process is shown both in cartoon and electrostatic potential surface modes. The positions of the active-site tyrosines are indicated by arrows when the tyrosines approach the target DNA backbone phosphates. The DNA backbone is in rose, the base pairs involved in sequence specific DNA recognition are in green, the nucleotides adjacent to the cleavage points are in purple in Licorice mode and the non-specific base pairs are in silver. The active-site tyrosines of the ParC dimer are represented in CPK mode in blue. The helix α3 is in cyan, the helix α4 is in red, the 100-122 loop is in yellow and the Gly 166-Pro 179 region is in orange. The movie was generated using VMD [50], Pov-Ray and PyMOL [53].
Date
Source Movie S1 from Laponogov I, Veselkov D, Sohi M, Pan X, Achari A, Yang C, Ferrara J, Fisher L, Sanderson M (2007). "Breakage-Reunion Domain of Streptococcus pneumoniae Topoisomerase IV: Crystal Structure of a Gram-Positive Quinolone Target". PLOS ONE. DOI:10.1371/journal.pone.0000301. PMID 17375187. PMC: 1810434.
Author Laponogov I, Veselkov D, Sohi M, Pan X, Achari A, Yang C, Ferrara J, Fisher L, Sanderson M
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current00:29, 14 November 20120.0 s, 682 × 480 (8.75 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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VP9 480P 0 bps Completed 01:12, 14 May 2023 29 s
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