Figure 5.
Modeling of interactions between Mis12cMtw1cand Ndc80c. (A) Molecular model of the interactions between the CC3 region of the Mis12cMtw1c stalk domain and the Spc24 and Spc25 RWD domains at interface (3) docked into the cryo-EM density map, showing density for select amino acid side chains relevant to the interaction. View is similar to Fig. 4 C. (B) Molecular model of the interactions between Mis12Mtw1_Spc24-helix and Dsn1Cterm-helix motifs with the Spc24 and Spc25 RWD domains at interface (4) docked into the cryo-EM density map, showing density for select amino acid side chains relevant to the interaction. View is similar to Fig. 4 D. (C) Structural alignment of the crystal structure of Spc24 and Spc25 RWD domains bound to Dsn1560-576 peptide (PDB: 5T6J) (Dimitrova et al., 2016) onto the Mis12cMtw1c and Spc24 and Spc25 experimental molecular models (this study). The Spc24 and Spc25 chains derived from 5T6J and this study are colored identically, while Dsn1Cterm-helix is colored distinctly according to whether it derives from 5T6J or this study. (D) AF2 model of the interaction between Spc24, Spc25, and Mis12cMtw1c (colored in red), structurally aligned against the Spc24, Spc25, and Mis12cMtw1c molecular models produced in this study (colored by chain). The prediction was performed using full-length and wild-type protein sequences for Spc24, Spc25, and Mis12cMtw1c subunits. (E) AF2 structure prediction presented in D colored by residue pLDDT score, with the PAE score plot shown in inset in the top right corner. PAE, predicted alignment error. Refer to the image caption for details. Panel A shows molecular model of C C 3 region interactions with S p c 24 and S p c 25 R W D domains docked into cryo-E M density, highlighting key residue contacts. Panel B shows molecular model of M i s 12 M t w 1 S p c 24-helix and D s n 1 C-terminal helix interactions with S p c 24 and S p c 25 at interface 4 within cryo-E M density. Panel C shows structural alignment of S p c 24:S p c 25 R W D domains with D s n 1 peptide (P D B 5 T 6 J) onto experimental M i s 12 c M t w 1 c complex. Panel D shows AlphaFold 2 predicted model aligned with experimental structure, comparing S p c 24, S p c 25 and M i s 12 c M t w 1 c interactions. Panel E shows AlphaFold 2 model colored by p L D D T confidence with P A E map inset indicating prediction reliability.

Modeling of interactions between Mis12c Mtw1c and Ndc80c. (A) Molecular model of the interactions between the CC3 region of the Mis12cMtw1c stalk domain and the Spc24 and Spc25 RWD domains at interface (3) docked into the cryo-EM density map, showing density for select amino acid side chains relevant to the interaction. View is similar to Fig. 4 C. (B) Molecular model of the interactions between Mis12Mtw1_Spc24-helix and Dsn1Cterm-helix motifs with the Spc24 and Spc25 RWD domains at interface (4) docked into the cryo-EM density map, showing density for select amino acid side chains relevant to the interaction. View is similar to Fig. 4 D. (C) Structural alignment of the crystal structure of Spc24 and Spc25 RWD domains bound to Dsn1560-576 peptide (PDB: 5T6J) (Dimitrova et al., 2016) onto the Mis12cMtw1c and Spc24 and Spc25 experimental molecular models (this study). The Spc24 and Spc25 chains derived from 5T6J and this study are colored identically, while Dsn1Cterm-helix is colored distinctly according to whether it derives from 5T6J or this study. (D) AF2 model of the interaction between Spc24, Spc25, and Mis12cMtw1c (colored in red), structurally aligned against the Spc24, Spc25, and Mis12cMtw1c molecular models produced in this study (colored by chain). The prediction was performed using full-length and wild-type protein sequences for Spc24, Spc25, and Mis12cMtw1c subunits. (E) AF2 structure prediction presented in D colored by residue pLDDT score, with the PAE score plot shown in inset in the top right corner. PAE, predicted alignment error.

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