ArticleMethods in enzymology2016
Deuterium Labeling Together with Contrast Variation Small-Angle Neutron Scattering Suggests How Skp Captures and Releases Unfolded Outer Membrane Proteins.
Article in Methods in enzymology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Software for small-angle neutron scattering contrast variation experiment planning and data analysis.Journal of applied crystallography · 2026Article
- Expression of soluble moloney murine leukemia virus-reverse transcriptase in Escherichia coli BL21 star (DE3) using autoinduction system.Molecular biology reports · 2024Article
- Generation of unfolded outer membrane protein ensembles defined by hydrodynamic properties.European biophysics journal : EBJ · 2023Article
- FkpA enhances membrane protein folding using an extensive interaction surface.Protein science : a publication of the Protein Society · 2023Article
- Small-angle neutron scattering contrast variation studies of biological complexes: Challenges and triumphs.Current opinion in structural biology · 2022Review
- DENSS-multiple: A structure reconstruction method using contrast variation of small-angle neutron scattering based on the DENSS algorithm.BBA advances · 2022Article
- EvolvingInternational journal of molecular sciences · 2021Article
- Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD.Nature communications · 2021Article
- SurA is a cryptically grooved chaperone that expands unfolded outer membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Domain interactions determine the conformational ensemble of the periplasmic chaperone SurA.Protein science : a publication of the Protein Society · 2020Article
- An integrative toolbox to unlock the structure and dynamics of protein-surfactant complexes.Nanoscale advances · 2020Article
- Affinity of Skp to OmpC revealed by single-molecule detection.Scientific reports · 2020Article
- Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients.Nature communications · 2020Article
- Periplasmic Chaperones and Prolyl Isomerases.EcoSal Plus · 2018Review
- Outer membrane protein folding from an energy landscape perspective.BMC biology · 2017Review
- Investigating Structure and Dynamics of Proteins in Amorphous Phases Using Neutron Scattering.Computational and structural biotechnology journal · 2017Review
- From Chaperones to the Membrane with a BAM!Trends in biochemical sciences · 2016Review
- Skp is a multivalent chaperone of outer-membrane proteins.Nature structural & molecular biology · 2016Article
- Protein folding in the cell envelope of Escherichia coli.Nature microbiology · 2016Review
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7 authors.
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Abstract
In Gram-negative bacteria, the chaperone protein Skp forms specific and stable complexes with membrane proteins while they are transported across the periplasm to the outer membrane. The jellyfish-like architecture of Skp is similar to the eukaryotic and archaeal prefoldins and the mitochondrial Tim chaperones, that is the α-helical "tentacles" extend from a β-strand "body" to create an internal cavity. Contrast variation small-angle neutron scattering (SANS) experiments on Skp alone in solution and bound in two different complexes to unfolded outer membrane proteins (uOMPs), OmpA and OmpW, demonstrate that the helical tentacles of Skp bind their substrate in a clamp-like mechanism in a conformation similar to that previously observed in the apo crystal structure of Skp. Deuteration of the uOMP component combined with contrast variation analysis allowed the shapes of Skp and uOMP as well as the location of uOMP with respect to Skp to be determined in both complexes. This represents unique information that could not be obtained without deuterium labeling of the uOMPs. The data yield the first direct structural evidence that the α-helical Skp tentacles move closer together on binding its substrate and that the structure of Skp is different when binding different uOMPs. This work presents, by example, a tutorial on performing SANS experiments using both deuterium labeling and contrast variation, including SANS theory, sample preparation, data collection, sample quality validation, data analysis, and structure modeling.
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