Fig. 1: Human MUTYH-TSAC structure and cancer-associated variants within the [4Fe-4S] cluster motif. | Nature Communications

Fig. 1: Human MUTYH-TSAC structure and cancer-associated variants within the [4Fe-4S] cluster motif.

From: Structure of human MUTYH and functional profiling of cancer-associated variants reveal an allosteric network between its [4Fe-4S] cluster cofactor and active site required for DNA repair

Fig. 1

A Global structure (shown in ribbons) highlighting functional domains, catalytic residues and the [4Fe-4S] cluster. The simulated annealing composite omit (gray) and anomalous difference (orange) maps were contoured at 1.1- and 6-sigma, respectively. Functional domains and motifs are indicated in different colors. A logo sequence shows the conservation of the cysteine ligands across archaea, bacteria and eukaryote MutY/MUTYH. B Frequency and distribution of pathogenic germline and somatic mutations mapped in MUTYH amino acid sequence. Domains and motifs are indicated with labels below amino acid numbering. Pathogenic somatic mutations (yellow) were obtained from the COSMIC database23. Pathogenic germline mutations were acquired from ExAC86 (blue), gnomAD87 (red) and TOPMED88 (green) databases. Reported frequencies were log-normalized (log base 10). Nonsense mutations are indicated with asterisk. Protein-protein interaction sites are shown with black labels. C Structural mapping of cancer-associated variants within the [4Fe-4S] cluster motif.

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