Dimerization of the type IV pilin from Pseudomonas aeruginosa strain K122-4 results in increased helix stability as measured by time-resolved hydrogen-deuterium exchange

Truncated pilin monomers from Pseudomonas aeruginosa strain K122-4 (ΔK122) have been shown to enter a monomer-dimer equilibrium in solution prior to oligomerization into protein nanotubes. Here, we examine the structural changes occurring between the monomeric and dimeric states of ΔK122 using time-...

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Published inStructural dynamics (Melville, N.Y.) Vol. 3; no. 1; p. 012001
Main Authors Lento, Cristina, Wilson, Derek J, Audette, Gerald F
Format Journal Article
LanguageEnglish
Published United States American Institute of Physics, Inc 01.01.2016
American Crystallographic Association
AIP Publishing LLC and ACA
Subjects
Biofilms
Chromatography
Deuterium
Dimerization
Equilibrium
Gram-positive bacteria
Hydrogen
Mass spectrometry
Monomers
Oligomerization
Proteins
Scientific imaging
SPECIAL TOPIC: PROTEIN DYNAMICS
Time measurement
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Abstract Truncated pilin monomers from Pseudomonas aeruginosa strain K122-4 (ΔK122) have been shown to enter a monomer-dimer equilibrium in solution prior to oligomerization into protein nanotubes. Here, we examine the structural changes occurring between the monomeric and dimeric states of ΔK122 using time-resolved hydrogen-deuterium exchange mass spectrometry. Based on levels of deuterium uptake, the N-terminal α-helix and the loop connecting the second and third strands of the anti-parallel β-sheet contribute significantly to pilin dimerization. Conversely, the antiparallel β-sheet and αβ loop region exhibit increased flexibility, while the receptor binding domain retains a rigid conformation in the equilibrium state.
AbstractList Truncated pilin monomers from Pseudomonas aeruginosa strain K122-4 (ΔK122) have been shown to enter a monomer-dimer equilibrium in solution prior to oligomerization into protein nanotubes. Here, we examine the structural changes occurring between the monomeric and dimeric states of ΔK122 using time-resolved hydrogen-deuterium exchange mass spectrometry. Based on levels of deuterium uptake, the N-terminal α-helix and the loop connecting the second and third strands of the anti-parallel β-sheet contribute significantly to pilin dimerization. Conversely, the antiparallel β-sheet and αβ loop region exhibit increased flexibility, while the receptor binding domain retains a rigid conformation in the equilibrium state.
Truncated pilin monomers from Pseudomonas aeruginosa strain K122-4 (ΔK122) have been shown to enter a monomer-dimer equilibrium in solution prior to oligomerization into protein nanotubes. Here, we examine the structural changes occurring between the monomeric and dimeric states of ΔK122 using time-resolved hydrogen-deuterium exchange mass spectrometry. Based on levels of deuterium uptake, the N-terminal α-helix and the loop connecting the second and third strands of the anti-parallel β-sheet contribute significantly to pilin dimerization. Conversely, the antiparallel β-sheet and αβ loop region exhibit increased flexibility, while the receptor binding domain retains a rigid conformation in the equilibrium state.
Author Wilson, Derek J
Audette, Gerald F
Lento, Cristina
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  surname: Wilson
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Snippet Truncated pilin monomers from Pseudomonas aeruginosa strain K122-4 (ΔK122) have been shown to enter a monomer-dimer equilibrium in solution prior to...
Truncated pilin monomers from Pseudomonas aeruginosa strain K122-4 (ΔK122) have been shown to enter a monomer-dimer equilibrium in solution prior to...
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StartPage 012001
SubjectTerms Biofilms
Chromatography
Deuterium
Dimerization
Equilibrium
Gram-positive bacteria
Hydrogen
Mass spectrometry
Monomers
Oligomerization
Proteins
Scientific imaging
SPECIAL TOPIC: PROTEIN DYNAMICS
Time measurement
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Title Dimerization of the type IV pilin from Pseudomonas aeruginosa strain K122-4 results in increased helix stability as measured by time-resolved hydrogen-deuterium exchange
URI https://www.ncbi.nlm.nih.gov/pubmed/26798830
https://www.proquest.com/docview/1953272551
https://search.proquest.com/docview/1760908647
https://pubmed.ncbi.nlm.nih.gov/PMC4711513
https://doaj.org/article/a452c8b6b815406dbccf600c4913e94a
Volume 3
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