Structural and functional characterization of TgpA, a critical protein for the viability of Pseudomonas aeruginosa.
Amino Acid Motifs
Bacterial Proteins
/ chemistry
Catalytic Domain
Cloning, Molecular
Crystallography, X-Ray
Escherichia coli
/ genetics
Gene Expression
Genetic Vectors
/ chemistry
Membrane Proteins
/ chemistry
Microbial Viability
Models, Molecular
Mutation
Peptidoglycan
/ chemistry
Periplasm
/ chemistry
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Pseudomonas aeruginosa
/ chemistry
Recombinant Fusion Proteins
/ chemistry
Substrate Specificity
Antibacterials
Cystic fibrosis
Heterologous expression
Peptidoglycans
Periplasmic proteins
Point mutations
X-ray crystallography
Journal
Journal of structural biology
ISSN: 1095-8657
Titre abrégé: J Struct Biol
Pays: United States
ID NLM: 9011206
Informations de publication
Date de publication:
01 03 2019
01 03 2019
Historique:
received:
29
08
2018
revised:
06
12
2018
accepted:
07
12
2018
pubmed:
2
1
2019
medline:
21
4
2020
entrez:
2
1
2019
Statut:
ppublish
Résumé
Pseudomonas aeruginosa is an opportunistic pathogen associated with severe diseases, such as cystic fibrosis. During an extensive search for novel essential genes, we identified tgpA (locus PA2873) in P. aeruginosa PAO1, as a gene playing a critical role in bacterial viability. TgpA, the translated protein, is an internal membrane protein with a periplasmic soluble domain, predicted to be endowed with a transglutaminase-like fold, hosting the Cys404, His448, and Asp464 triad. We report here that Cys404 mutation hampers the essential role of TgpA in granting P. aeruginosa viability. Moreover, we present the crystal structure of the TgpA periplasmic domain at 1.6 Å resolution as a first step towards structure-activity analysis of a new potential target for the discovery of antibacterial compounds.
Identifiants
pubmed: 30599211
pii: S1047-8477(18)30317-4
doi: 10.1016/j.jsb.2018.12.004
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Membrane Proteins
0
Peptidoglycan
0
Recombinant Fusion Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
18-25Informations de copyright
Copyright © 2019 The Authors. Published by Elsevier Inc. All rights reserved.