Fig. 5: Ty3 CCD-CTD extended linker creates a platform for TFIIIB assembly. | Nature Communications

Fig. 5: Ty3 CCD-CTD extended linker creates a platform for TFIIIB assembly.

From: Structural basis of Ty3 retrotransposon integration at RNA Polymerase III-transcribed genes

Fig. 5

a Detailed view of the orientation adopted by the CCD-CTD linker of Ty3 integrase outer subunit. Ty3 extended linker adopts a peripheral orientation that creates a platform for the interaction between Ty3 CTD and CHD domains (purple ribbon) and TFIIIB transcription factor (pink and green surfaces). The outer catalytic core domain (CCD) and the DNA molecules are shown as transparent ribbons. b As in a but for Respiratory Syncytial Virus (RSV, PDB code: 5EJK). c As in a but for Human Immunodeficiciency Virus (HIV, PDB code: 5U1C). Binding of LEDGF/p75 transcription factor (green ribbon) to HIV could be mediated by a similar region than in the Brf1-IN interaction, which highlights a potential hot-spot for host-integrase recognition events. d As in a but for Mouse Mammary Tumor Virus (MMTV, PDB code: 3JCA). e As in a but for Prototype Foamy Virus (PFV, PDB code: 3OS0). f As in a but for Human T-lymphotropic Virus Type 1 (HLTV, PDB code: 6VOY). Binding of CCD-CTD linker to B56γ (green ribbon) is represented.

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