ArticleProtein science : a publication of the Protein Society1998
Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers.
Article in Protein science : a publication of the Protein Society, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 78 citations in OpenAlex.
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Pore-forming toxins: ancient, but never really out of fashion.Nature reviews. Microbiology · 2016Review
- Cardiolipin interaction with subunit c of ATP synthase: solid-state NMR characterization.Biochimica et biophysica acta · 2015Article
- Membrane partitioning of the pore-forming domain of colicin A. Role of the hydrophobic helical hairpin.Biophysical journal · 2013Article
- Article
- alphaB-crystallin: a hybrid solid-state/solution-state NMR investigation reveals structural aspects of the heterogeneous oligomer.Journal of molecular biology · 2009Article
- Continuity conditions and torsion angles from ssNMR orientational restraints.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2008Article
- Identifying anisotropic constraints in multiply labeled bacteriorhodopsin by 15N MAOSS NMR: a general approach to structural studies of membrane proteins.Biophysical journal · 2004Article
- Structural studies of apoptosis and ion transport regulatory proteins in membranes.Magnetic resonance in chemistry : MRC · 2004Article
- Assembly of colicin A in the outer membrane of producing Escherichia coli cells requires both phospholipase A and one porin, but phospholipase A is sufficient for secretion.Journal of bacteriology · 2002Article
- Structure and topology of a peptide segment of the 6th transmembrane domain of the Saccharomyces cerevisae alpha-factor receptor in phospholipid bilayers.Biopolymers · 2001Article
- Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy.Biophysical journal · 2001Article
- A simple approach to membrane protein secondary structure and topology based on NMR spectroscopy.Biophysical journal · 2001Article
- Nuclear magnetic resonance of membrane-associated peptides and proteins.Methods in enzymology · 2001Review
- A solid-state NMR index of helical membrane protein structure and topology.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2000Article
- Correlation of the structural and functional domains in the membrane protein Vpu from HIV-1.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Orientation of cecropin A helices in phospholipid bilayers determined by solid-state NMR spectroscopy.Biophysical journal · 1999Article
- Dilute spin-exchange assignment of solid-state NMR spectra of oriented proteins: acetylcholine M2 in bilayers.Journal of biomolecular NMR · 1999Article
- Solid-state NMR triple-resonance backbone assignments in a protein.Journal of biomolecular NMR · 1999Article
- Structure in the channel forming domain of colicin E1 bound to membranes: the 402-424 sequence.Protein science : a publication of the Protein Society · 1999Article
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5 authors at 2 institutions in 1 country.
Funding
Abstract
The colicin E1 channel polypeptide was shown to be organized anisotropically in membranes by solid-state NMR analysis of samples of uniformly 15N-labeled protein in oriented planar phospholipid bilayers. The 190 residue C-terminal colicin E1 channel domain is the largest polypeptide to have been characterized by 15N solid-state NMR spectroscopy in oriented membrane bilayers. The 15N-NMR spectra of the colicin E1 show that: (1) the structure and dynamics are independent of anionic lipid content in both oriented and unoriented samples; (2) assuming the secondary structure of the polypeptide is helical, there are both trans-membrane and in-plane helical segments; (3) trans-membrane helices account for approximately 20-25% of the channel polypeptide, which is equivalent to 38-48 residues of the 190-residue polypeptide. The results of the two-dimensional PISEMA spectrum are interpreted in terms of a single trans-membrane helical hairpin inserted into the bilayer from each channel molecule. These data are also consistent with this helical hairpin being derived from the 38-residue hydrophobic segment near the C-terminus of the colicin E1 channel polypeptide.
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