Structure and membrane-targeting of a Bordetella pertussis effector N-terminal domain.
Amino Acid Sequence
/ genetics
Bacterial Proteins
/ chemistry
Bordetella pertussis
/ metabolism
Crystallography, X-Ray
/ methods
Cytotoxicity, Immunologic
/ physiology
Membrane Proteins
/ metabolism
Molecular Chaperones
/ metabolism
Phosphatidylinositols
/ metabolism
Protein Binding
/ physiology
Scattering, Small Angle
Structure-Activity Relationship
Type III Secretion Systems
/ metabolism
X-Ray Diffraction
/ methods
Bordetella
Effector
Membrane targeting
NMR spectroscopy
Type 3 secretion system
X-ray crystallography
Journal
Biochimica et biophysica acta. Biomembranes
ISSN: 1879-2642
Titre abrégé: Biochim Biophys Acta Biomembr
Pays: Netherlands
ID NLM: 101731713
Informations de publication
Date de publication:
01 12 2019
01 12 2019
Historique:
received:
29
05
2019
revised:
05
08
2019
accepted:
22
08
2019
pubmed:
6
9
2019
medline:
3
3
2020
entrez:
6
9
2019
Statut:
ppublish
Résumé
BteA, a 69-kDa cytotoxic protein, is a type III secretion system (T3SS) effector in the classical Bordetella, the etiological agents of pertussis and related mammalian respiratory diseases. Like other cytotoxicity-mediating effectors, BteA uses its multifunctional N-terminal domain to target phosphatidylinositol (PI)-rich microdomains in the host membrane. Despite their structural similarity, T3SS effectors exhibit a variable range of membrane interaction modes, and currently only limited structural information is available for the BteA membrane-targeting domain and the molecular mechanisms underlying its function. Employing a synergistic combination of structural methods, here we determine the structure of this functional domain and uncover key molecular determinants mediating its interaction with membranes. Residues 29-121 of BteA form an elongated four-helix bundle packed against two shorter perpendicular helices, the second of which caps the domain in a critical 'tip motif'. A flexible region preceding the BteA helical bundle contains the characteristic β-motif required for binding its cognate chaperone BtcA. We show that BteA targets PI(4,5)P
Identifiants
pubmed: 31487494
pii: S0005-2736(19)30200-7
doi: 10.1016/j.bbamem.2019.183054
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Membrane Proteins
0
Molecular Chaperones
0
Phosphatidylinositols
0
Type III Secretion Systems
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
183054Informations de copyright
Copyright © 2019 Elsevier B.V. All rights reserved.