Pinpointing the L-phenylalanine binding sites of TyrR using biosensors and computer-aided simulation.
Biotechnol Lett
; 41(3): 401-408, 2019 Mar.
Article
in En
| MEDLINE
| ID: mdl-30680497
ABSTRACT
OBJECTIVES:
To determine the binding sites for L-phenylalanine in TyrR protein via a rational mutation analysis combining biosensors and computer-aided simulation.RESULTS:
TyrR 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.CONCLUSIONS:
Residues 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.Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Phenylalanine
/
Repressor Proteins
/
Escherichia coli Proteins
/
Escherichia coli
Type of study:
Prognostic_studies
Language:
En
Journal:
Biotechnol Lett
Year:
2019
Document type:
Article