Dynamic aspects of pressure and temperature-stabilized intermediates of outer surface protein A.
Animals
Antigens, Surface
/ chemistry
Arthropod Proteins
/ chemistry
Bacterial Outer Membrane Proteins
/ chemistry
Bacterial Vaccines
/ chemistry
Binding Sites
Borrelia
/ chemistry
Cloning, Molecular
Escherichia coli
/ genetics
Gene Expression
Genetic Vectors
/ chemistry
Intrinsically Disordered Proteins
/ chemistry
Lipoproteins
/ chemistry
Molecular Dynamics Simulation
Nuclear Magnetic Resonance, Biomolecular
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Folding
Protein Interaction Domains and Motifs
Receptors, Cell Surface
/ chemistry
Recombinant Proteins
/ chemistry
Thermodynamics
Ticks
/ microbiology
OspA
intermediates
nuclear magnetic resonance
paramagnetic relaxation enhancement
pressure
Journal
Proteins
ISSN: 1097-0134
Titre abrégé: Proteins
Pays: United States
ID NLM: 8700181
Informations de publication
Date de publication:
11 2020
11 2020
Historique:
received:
06
04
2020
revised:
05
05
2020
accepted:
06
06
2020
pubmed:
11
6
2020
medline:
9
2
2021
entrez:
11
6
2020
Statut:
ppublish
Résumé
Structural characterization of alternatively folded and partially disordered protein conformations remains challenging. Outer surface protein A (OspA) is a pivotal protein in Borrelia infection, which is the etiological agent of Lyme disease. OspA exists in equilibrium with intermediate conformations, in which the central and the C-terminal regions of the protein have lower stabilities than the N-terminal. Here, we characterize pressure- and temperature-stabilized intermediates of OspA by nuclear magnetic resonance spectroscopy combined with paramagnetic relaxation enhancement (PRE). We found that although the C-terminal region of the intermediate was partially disordered, it retains weak specific contact with the N-terminal region, owing to a twist of the central β-sheet and increased flexibility in the polypeptide chain. The disordered C-terminal region of the pressure-stabilized intermediate was more compact than that of the temperature-stabilized form. Further, molecular dynamics simulation demonstrated that temperature-induced disordering of the β-sheet was initiated at the C-terminal region and continued through to the central region. An ensemble of simulation snapshots qualitatively described the PRE data from the intermediate and indicated that the intermediate structures of OspA may expose tick receptor-binding sites more readily than does the basic folded conformation.
Substances chimiques
Antigens, Surface
0
Arthropod Proteins
0
Bacterial Outer Membrane Proteins
0
Bacterial Vaccines
0
Intrinsically Disordered Proteins
0
Lipoproteins
0
OspA protein
0
Receptors, Cell Surface
0
Recombinant Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1423-1433Informations de copyright
© 2020 Wiley Periodicals LLC.
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