Figure 5. Analysis of RpoE10 (Del 1) model. Structural models A) RpoE10 and its deletion derivatives B) RpoE10 (Del1) and C) RpoE10(Del2). B inset view: Snapshots of the RpoE10(Del1) model structure at various time intervals illustrating the stabilization of the DGGG motif and tethering of the σ2-σ4 domain is partially truncated c-terminal SnoaL_2 domain. The ball and stick model of residues depicts the 200DGGG2G03 (magenta) interactions with linker region residues (83WLPEP87, green color). The RpoE10 structure with intact SnoaL_2 domain showing the interaction between the WLPEP, DGGGR, and NPDKV motifs (interactions are shown in Figure 1A). (C) Model of the RpoE10(Del2) illustrating the loss of interactions between the DGGGR and WLPEP motifs in the C-terminal truncated SnoaL_2 domain. D) Root-mean-square deviation profile of RpoE10(Del1) generated from 200 ns MD simulations trajectory. Truncated SnoaL_2 domain influence the compactness of σ2 -σ4 conformation and influence the backbone conformations of σ2 -σ4 domains. E) RpoE10 Del1) showed the stable conformations of the σ2- σ4 domain across a large number of conformers. F) The schematic diagram depicts the impact of compactness on promoter activation. Compact and homogenous σ2-σ4 domain conformers in RpoE10(Del1) suggest that the truncated SnoaL_2 domain-containing DGGG motif alone may constraint RpoE10 to a compact and stable structure. G) Compactness analysis using the radius of gyration calculations of individual σ2, σ4, SnoaL_2, and combined σ2-σ4 domain for truncated Snoal_2 domain of RpoE10(Del1).H) A plot of minimum distance calculated between σ2 and σ4 domain for RpoE10 (Del1). I) A comparative RMSF plot of RpoE10(Del1) with RpoE10 and RpoE10 (Mut1). An arrow marks the differential and key residue positions showing distinct RMSF peaks. These residues are mapped (in black color) onto the structure of the RpoE10 model (Figure 4A).