Identification of a pyrophosphate-dependent kinase and its donor selectivity determinants
| Autor: | Takaaki Sato, Masahiro Fujihashi, Ryuhei Nagata, Haruyuki Atomi, Kunio Miki |
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| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular 0301 basic medicine Science Protein domain General Physics and Astronomy Sequence alignment Crystallography X-Ray Biochemistry Article General Biochemistry Genetics and Molecular Biology 03 medical and health sciences Protein Domains Transferase Amino Acid Sequence Amino Acids Binding site Ribokinase lcsh:Science Peptide sequence Binding Sites Multidisciplinary Base Sequence Sequence Homology Amino Acid 030102 biochemistry & molecular biology Chemistry Kinase General Chemistry Chemical biology Diphosphates Kinetics Phosphotransferases (Alcohol Group Acceptor) 030104 developmental biology Structural biology Mutation lcsh:Q |
| Zdroj: | Nature Communications, Vol 9, Iss 1, Pp 1-8 (2018) Nature Communications |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-018-04201-z |
| Popis: | 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. 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. |
| Databáze: | OpenAIRE |
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