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Pinpointing the l-phenylalanine binding sites of TyrR using biosensors and computer-aided simulation

Authors
  • Bai, Danyang1, 2
  • Ding, Dongqin2, 3, 4
  • Li, Jinlong2
  • Cong, Lina1
  • Zhang, Dawei2, 3, 4
  • 1 Dalian Polytechnic University, School of Biological Engineering, Dalian, 116034, People’s Republic of China , Dalian (China)
  • 2 Tianjin Institutes of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, 300308, People’s Republic of China , Tianjin (China)
  • 3 Chinese Academy of Sciences, Key Laboratories of Systems Microbial Biotechnology, Tianjin, 300308, People’s Republic of China , Tianjin (China)
  • 4 University of Chinese Academy of Sciences, Beijing, 100049, People’s Republic of China , Beijing (China)
Type
Published Article
Journal
Biotechnology Letters
Publisher
Springer-Verlag
Publication Date
Jan 24, 2019
Volume
41
Issue
3
Pages
401–408
Identifiers
DOI: 10.1007/s10529-019-02645-x
Source
Springer Nature
Keywords
License
Yellow

Abstract

ObjectivesTo determine the binding sites for l-phenylalanine in TyrR protein via a rational mutation analysis combining biosensors and computer-aided simulation.ResultsTyrR protein of Escherichia coli is the chief transcriptional regulator of several genes essential for the biosynthesis and transport of aromatic amino acids. The identification of ligand-binding sites is often the starting point for protein function annotation and structure-based protein design. Here we combined computer-aided prediction methods and biosensors to identify the ligand-binding sites for l-Phe in TyrR protein.ConclusionsResidues at positions 160, 173 and 184 of TyrR protein are important for transcriptional activation of target genes tyrP induced by l-Phe, which indicates that they are the bona fide l-Phe binding sites of TyrR protein.

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