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Crystal structure of the N‐terminal domain of VqsR from Pseudomonas aeruginosa at 2.1 Å resolution
Author(s) -
He Qing,
Wang Kang,
Su Tiantian,
Wang Feng,
Gu Lichuan,
Xu Sujuan
Publication year - 2017
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x17009025
Subject(s) - quorum sensing , pseudomonas aeruginosa , chemistry , regulator , homoserine , receptor , pas domain , helix turn helix , structural similarity , c terminus , dna , sequence alignment , peptide sequence , biology , genetics , gene , biochemistry , repressor , amino acid , transcription factor , bacteria , virulence
VqsR is a quorum‐sensing (QS) transcriptional regulator which controls QS systems ( las , rhl and pqs ) by directly downregulating the expression of qscR in Pseudomonas aeruginosa . As a member of the LuxR family of proteins, VqsR shares the common motif of a helix–turn–helix (HTH)‐type DNA‐binding domain at the C‐terminus, while the function of its N‐terminal domain remains obscure. Here, the crystal structure of the N‐terminal domain of VqsR (VqsR‐N; residues 1–193) was determined at a resolution of 2.1 Å. The structure is folded into a regular α–β–α sandwich topology, which is similar to the ligand‐binding domain (LBD) of the LuxR‐type QS receptors. Although their sequence similarity is very low, structural comparison reveals that VqsR‐N has a conserved enclosed cavity which could recognize acyl‐homoserine lactones (AHLs) as in other LuxR‐type AHL receptors. The structure suggests that VqsR could be a potential AHL receptor.