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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)

Submitter: 津田 栄

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