pbio.3002459.s002.tiff (1.73 MB)
Comparison of the 27 SSM library residues from our SWISS-MODEL and an AlphaFold2 model.
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posted on 2024-01-18, 18:40 authored by Martin Bonin, Antonia L. Irion, Anika Jürß, Sergi Pascual, Stefan Cord-Landwehr, Antoni Planas, Bruno M. MoerschbacherThe AlphaFold2 model from the AlphaFold Protein Structure Database [35,36] was aligned to our SWISS-MODEL with an RMSD = 1.341 Å on all atoms and an RMSD = 0.782 Å on the 27 SSM library amino acids. Our SWISS-MODEL is shown with blue, and the AlphaFold2 model is shown with red carbon atoms, respectively. For an easier overall comparison, the other colors and labels are reused from Fig 1.
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several amino acidssaturation mutagenesis libraryincreases enzyme activitydetailed activity screeningcrucial interactions alongmolecular dynamics simulationshighly specific bindingalso significantly changessubsite − 2>- acetylating polyglucosaminediv >< pcould clearly showsubsite − 1subsite preferences influence− 1subsite preferencesmolecular basischanges composition>- acetylglucosamine>- acetylatevaluable toolsubstrate matchingproduce chitosanspestalotiopsis oligomeric productsnonrandom positionsnonrandom distributionn generate tailordepth viewchitosans producedchitin deacetylaseschitin deacetylasebinding sitebesides elucidating3 residues
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