Characterization of microbial antifreeze protein with intermediate activity suggests that a bound-water network is essential for hyperactivity
| Autor: | Sakae Tsuda, Tatsuya Arai, Hidemasa Kondo, N. M.-Mofiz Uddin Khan |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Gene isoform Biomaterials - proteins Protein Conformation Science Phenylalanine Crystal structure Molecular Dynamics Simulation Article Fungal Proteins 03 medical and health sciences Structure-Activity Relationship Antifreeze protein Antifreeze Proteins Side chain Molecule Bound water Protein Interaction Domains and Motifs Amino Acid Sequence Multidisciplinary Binding Sites 030102 biochemistry & molecular biology biology Chemistry Basidiomycota Ice Water biology.organism_classification Liquid Crystals Molecular Docking Simulation 030104 developmental biology Typhula ishikariensis Mutation Biophysics Medicine Structural biology Protein Binding |
| Zdroj: | Scientific Reports Scientific Reports, Vol 11, Iss 1, Pp 1-15 (2021) |
| ISSN: | 2045-2322 |
| Popis: | Antifreeze proteins (AFPs) inhibit ice growth by adsorbing onto specific ice planes. Microbial AFPs show diverse antifreeze activity and ice plane specificity, while sharing a common molecular scaffold. To probe the molecular mechanisms responsible for AFP activity, we here characterized the antifreeze activity and crystal structure of TisAFP7 from the snow mold fungus Typhula ishikariensis. TisAFP7 exhibited intermediate activity, with the ability to bind the basal plane, compared with a hyperactive isoform TisAFP8 and a moderately active isoform TisAFP6. Analysis of the TisAFP7 crystal structure revealed a bound-water network arranged in a zigzag pattern on the surface of the protein’s ice-binding site (IBS). While the three AFP isoforms shared the water network pattern, the network on TisAFP7 IBS was not extensive, which was likely related to its intermediate activity. Analysis of the TisAFP7 crystal structure also revealed the presence of additional water molecules that form a ring-like network surrounding the hydrophobic side chain of a crucial IBS phenylalanine, which might be responsible for the increased adsorption of AFP molecule onto the basal plane. Based on these observations, we propose that the extended water network and hydrophobic hydration at IBS together determine the TisAFP activity. |
| Databáze: | OpenAIRE |
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