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Title: Identification of a pyrophosphate-dependent kinase and its donor selectivity determinants
Authors: Nagata, Ryuhei
Fujihashi, Masahiro  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0002-6882-9697 (unconfirmed)
Sato, Takaaki
Atomi, Haruyuki  kyouindb  KAKEN_id
Miki, Kunio
Author's alias: 永田, 隆平
藤橋, 雅宏
佐藤, 喬章
跡見, 晴幸
三木, 邦夫
Keywords: Biochemistry
Chemical biology
Structural biology
Issue Date: 2-May-2018
Publisher: Springer Nature
Journal title: Nature Communications
Volume: 9
Thesis number: 1765
Abstract: Almost all kinases utilize ATP as their phosphate donor, while a few kinases utilize pyrophosphate (PPi) instead. PPi-dependent kinases are often homologous to their ATP-dependent counterparts, but determinants of their different donor specificities remain unclear. We identify a PPi-dependent member of the ribokinase family, which differs from known PPi-dependent kinases, and elucidate its PPi-binding mode based on the crystal structures. Structural comparison and sequence alignment reveal five important residues: three basic residues specifically recognizing PPi and two large hydrophobic residues occluding a part of the ATP-binding pocket. Two of the three basic residues adapt a conserved motif of the ribokinase family for the PPi binding. Using these five key residues as a signature pattern, we discover additional PPi-specific members of the ribokinase family, and thus conclude that these residues are the determinants of PPi-specific binding. Introduction of these residues may enable transformation of ATP-dependent ribokinase family members into PPi-dependent enzymes.
Description: お財布にも環境にもやさしい化学反応を発見 --新規リン酸化酵素がATPでなくピロリン酸を利用する仕組み--. 京都大学プレスリリース. 2018-05-16.
Rights: © The Author(s) 2018. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
URI: http://hdl.handle.net/2433/231115
DOI(Published Version): 10.1038/s41467-018-04201-z
PubMed ID: 29720581
Related Link: http://www.kyoto-u.ac.jp/ja/research/research_results/2018/180502_2.html
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