7DC5
Crystal structure of fungal antifreeze protein with intermediate activity
7DC5 の概要
| エントリーDOI | 10.2210/pdb7dc5/pdb |
| 分子名称 | Antifreeze protein, SULFATE ION (3 entities in total) |
| 機能のキーワード | right-handed beta-helix, beta-solenoid, ice-binding protein, thermal hysteresis protein, ice-structuring protein, antifreeze protein |
| 由来する生物種 | Typhula ishikariensis (Gray snow mold fungus) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 44631.86 |
| 構造登録者 | |
| 主引用文献 | Khan, N.M.U.,Arai, T.,Tsuda, S.,Kondo, H. Characterization of microbial antifreeze protein with intermediate activity suggests that a bound-water network is essential for hyperactivity. Sci Rep, 11:5971-5971, 2021 Cited by PubMed Abstract: 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. PubMed: 33727595DOI: 10.1038/s41598-021-85559-x 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.54 Å) |
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