Fig. 4: ELOF1 suppresses CSA mobility and repositions UVSSA’s VHS domain to facilitate precise CRL4CSA assembly.
From: Molecular model of TFIIH recruitment to the transcription-coupled repair machinery
Integrative structural models of (a), the TCR–CSA–DDB1, (b), TCR–CSA–DDB1–VHS, and (c), TCR–CSA–DDB1–VHS–ELOF1 complexes. Proteins are labeled and color-coded as follows: CSB (magenta), CSA (green), DDB1 (gold), UVSSA (purple), SPT6 (light brown), Pol II (gray). Template and non-template DNA is shown in cyan and blue; RNA is in red. Computed B-factors are mapped onto the structures of (d), the TCR–CSA–DDB1, (e), TCR–CSA–DDB1–VHS, and (f), TCR–CSA–DDB1–VHS–ELOF1 complexes. Rigid and flexible regions are color-coded from blue to red, respectively. g Zoomed-in view of the CSA–VHS–ELOF1 module. Protein interfaces are indicated by black dashed lines. h Comparison of the positioning of the CSA–VHS–DDB1 module in the presence/absence of ELOF1. In the model without ELOF1, CSA, VHS, and DDB1 are colored in green, gold, and purple, respectively. In the model with ELOF1 (dark purple), CSA, VHS, and DDB1 are colored in violet, orange, and light green. The extent of the conformational transition between the two states is indicated by black arrows.
