ArticleJournal of molecular biology2011
Structure of the BamC two-domain protein obtained by Rosetta with a limited NMR data set.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.Chemical reviews · 2026Review
- ATP-independent assembly machinery of bacterial outer membranes: BAM complex structure and function set the stage for next-generation therapeutics.Protein science : a publication of the Protein Society · 2024Review
- β-Barrel Assembly Machinery (BAM) Complex as Novel Antibacterial Drug Target.Molecules (Basel, Switzerland) · 2023Review
- Divide and Conquer: A Tailored Solid-state NMR Approach to Study Large Membrane Protein Complexes.Angewandte Chemie (International ed. in English) · 2022Article
- Building Better Barrels - β-barrel Biogenesis and Insertion in Bacteria and Mitochondria.Journal of molecular biology · 2021Review
- The big BAM theory: An open and closed case?Biochimica et biophysica acta. Biomembranes · 2020Review
- Article
- Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra.Nature communications · 2018Article
- Transmembrane β-barrels: Evolution, folding and energetics.Biochimica et biophysica acta. Biomembranes · 2017Review
- Structural snapshots of the β-barrel assembly machinery.The FEBS journal · 2017Review
- The β-barrel assembly machinery in motion.Nature reviews. Microbiology · 2017Review
- Flexibility in the Periplasmic Domain of BamA Is Important for Function.Structure (London, England : 1993) · 2017Article
- Article
- The Structure of a BamA-BamD Fusion Illuminates the Architecture of the β-Barrel Assembly Machine Core.Structure (London, England : 1993) · 2016Article
- Fitting the Pieces of the β-Barrel Assembly Machinery Complex.Biochemistry · 2015Review
- Characterization of the insertase BamA in three different membrane mimetics by solution NMR spectroscopy.Journal of biomolecular NMR · 2015Article
- Crystal structure of BamB bound to a periplasmic domain fragment of BamA, the central component of the β-barrel assembly machine.The Journal of biological chemistry · 2015Article
- TDP-43 N terminus encodes a novel ubiquitin-like fold and its unfolded form in equilibrium that can be shifted by binding to ssDNA.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Less is more: structures of difficult targets with minimal constraints.Structure (London, England : 1993) · 2014Article
- The structure of mouse cytomegalovirus m04 protein obtained from sparse NMR data reveals a conserved fold of the m02-m06 viral immune modulator family.Structure (London, England : 1993) · 2014Article
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7 authors.
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Abstract
The CS-RDC-NOE Rosetta program was used to generate the solution structure of a 27-kDa fragment of the Escherichia coli BamC protein from a limited set of NMR data. The BamC protein is a component of the essential five-protein β-barrel assembly machine in E. coli. The first 100 residues in BamC were disordered in solution. The Rosetta calculations showed that BamC₁₀₁₋₃₄₄ forms two well-defined domains connected by an ~18-residue linker, where the relative orientation of the domains was not defined. Both domains adopt a helix-grip fold previously observed in the Bet v 1 superfamily. ¹⁵N relaxation data indicated a high degree of conformational flexibility for the linker connecting the N-terminal domain and the C-terminal domain in BamC. The results here show that CS-RDC-NOE Rosetta is robust and has a high tolerance for misassigned nuclear Overhauser effect restraints, greatly simplifying NMR structure determinations.
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