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The weight of structural evidence favors the idea that an ATP-dependent ligase would be the ancestral condition from which NAD+-dependent ligases advanced, by acquisition of a specialized structural area (Ia) that binds the NMN leaving team. All regarded NAD+-dependent ligases have domain Ia, and they cannot use ATP like a substrate for ligase adenylylation, presumably for the reason that LigA enzymes deficiency “motif IV” of your OB area, the part of ATP-dependent DNA ligases that is believed to interact with the PPi leaving group of ATP (five, 19). This “both/or” circumstance of DNA ligase substrate specificity has become roiled by many seemingly conflicting studies in regards to the nucleotide specificity of archaeal DNA ligases.
DNA binding entails a nearly 180° rotation of the OB area all around a swivel (denoted because of the black arrow
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S3), nevertheless the topology in the LigA clamp is starkly various from that of your clamps formed by ChVLig and HuLig1. The kissing contacts that shut the LigA clamp are sui generis
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