ArticleNature structural & molecular biology2013
Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp.
Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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Who cites it
71 citing papers in PubMed, 138 citations in OpenAlex.
- Monitoring Membrane Protein Folding Assisted by Insertases and Translocases Using AFM-Based Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Dynamic disorder is crucial for mitochondrial protein import.Protein science : a publication of the Protein Society · 2026Review
- Architecture and conformational dynamics of the BAM-SurA holo insertase complex.Science advances · 2025Article
- Periplasmic Chaperones: Outer Membrane Biogenesis and Envelope Stress.Annual review of microbiology · 2024Review
- Dual client binding sites in the ATP-independent chaperone SurA.Nature communications · 2024Article
- Structural basis of substrate recognition and allosteric activation of the proapoptotic mitochondrial HtrA2 protease.Nature communications · 2024Article
- Structural insights into the mechanism of protein transport by the Type 9 Secretion System translocon.Nature microbiology · 2024Article
- Dynamic stability of Sgt2 enables selective and privileged client handover in a chaperone triad.Nature communications · 2024Article
- High-throughput screening of BAM inhibitors in native membrane environment.Nature communications · 2023Article
- Thumb-domain dynamics modulate the functional repertoire of DNA-Polymerase IV (DinB).Nucleic acids research · 2023Article
- FkpA enhances membrane protein folding using an extensive interaction surface.Protein science : a publication of the Protein Society · 2023Article
- Large Chaperone Complexes Through the Lens of Nuclear Magnetic Resonance Spectroscopy.Annual review of biophysics · 2022Review
- Chaperones Skp and SurA dynamically expand unfolded OmpX and synergistically disassemble oligomeric aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The sacrificial adaptor protein Skp functions to remove stalled substrates from the β-barrel assembly machine.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The periplasmic chaperone Skp prevents misfolding of the secretory lipase A fromFrontiers in molecular biosciences · 2022Article
- The role of heat shock proteins in preventing amyloid toxicity.Frontiers in molecular biosciences · 2022Review
- Structural basis of DegP protease temperature-dependent activation.Science advances · 2021Article
- Altered ceramide metabolism is a feature in the extracellular vesicle-mediated spread of alpha-synuclein in Lewy body disorders.Acta neuropathologica · 2021Article
- Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation.mBio · 2021Article
- Bacterial Outer Membrane Proteins Are Targeted to the Bam Complex by Two Parallel Mechanisms.mBio · 2021Article
11 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The biogenesis of integral outer-membrane proteins (OMPs) in Gram-negative bacteria requires molecular chaperones that prevent the aggregation of OMP polypeptides in the aqueous periplasmic space. How these energy-independent chaperones interact with their substrates is not well understood. We have used high-resolution NMR spectroscopy to examine the conformation and dynamics of the Escherichia coli periplasmic chaperone Skp and two of its complexes with OMPs. The Skp trimer constitutes a flexible architectural scaffold that becomes more rigid upon substrate binding. The OMP substrates populate a dynamic conformational ensemble with structural interconversion rates on the submillisecond timescale. The global lifetime of the chaperone-substrate complex is seven orders of magnitude longer, emerging from the short local lifetimes by avidity. The dynamic state allows for energy-independent substrate release and provides a general paradigm for the conformation of OMP polypeptides bound to energy-independent chaperones.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.