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Polypentagonal ice-like water networks emerge solely in an activity-improved variant of ice-binding protein
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Title: | Polypentagonal ice-like water networks emerge solely in an activity-improved variant of ice-binding protein |
Authors: | Mahatabuddin, Sheikh Browse this author | Fukami, Daichi Browse this author | Arai, Tatsuya Browse this author | Nishimiya, Yoshiyuki Browse this author →KAKEN DB | Shimizu, Rumi Browse this author | Shibazaki, Chie Browse this author | Kondo, Hidemasa Browse this author →KAKEN DB | Adachi, Motoyasu Browse this author | Tsuda, Sakae Browse this author →KAKEN DB |
Keywords: | hydration shell | ice-binding protein | crystal structure | water cluster | polypentagonal waters |
Issue Date: | 22-May-2018 |
Publisher: | National Academy of Sciences. |
Journal Title: | Proceedings of the National Academy of Sciences of the United States of America (PNAS) |
Volume: | 115 |
Issue: | 21 |
Start Page: | 5456 |
End Page: | 5461 |
Publisher DOI: | 10.1073/pnas.1800635115 |
PMID: | 29735675 |
Abstract: | Polypentagonal water networks were recently observed in a protein capable of binding to ice crystals, or ice-binding protein (IBP). To examine such water networks and clarify their role in ice-binding, we determined X-ray crystal structures of a 65-residue defective isoform of a Zoarcidae-derived IBP (wild type, WT) and its five single mutants (A20L, A20G, A20T, A20V, and A20I). Polypentagonal water networks composed of similar to 50 semiclathrate waters were observed solely on the strongest A20I mutant, which appeared to include a tetrahedral water cluster exhibiting a perfect position match to the (1010) first prism plane of a single ice crystal. Inclusion of another symmetrical water cluster in the poly-pentagonal network showed a perfect complementarity to the waters constructing the (2021) pyramidal ice plane. The order of ice-binding strength was A20L < A20G < WT < A20T < A20V < A20I, where the top three mutants capable of binding to the first prism and the pyramidal ice planes commonly contained a bifurcated gamma-CH3 group. These results suggest that a fine-tuning of the surface of Zoarcidae-derived IBP assisted by a side-chain group regulates the holding property of its polypentagonal water network, the function of which is to freeze the host protein to specific ice planes. |
Rights: | Copyright (C) 2018 the Author(s). Published by PNAS | https://creativecommons.org/licenses/by-nc-nd/4.0/ |
Type: | article |
URI: | http://hdl.handle.net/2115/71437 |
Appears in Collections: | 生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 津田 栄
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