Crystal structure of Staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel
暂无分享,去创建一个
Kenji Yokota | Rich Olson | Eric Gouaux | E. Gouaux | R. Olson | Y. Kamio | K. Yokota | Yoshiyuki Kamio | H. Nariya | Hirofumi Nariya
[1] G. Duportail,et al. Pore formation by a two-component leukocidin from Staphylococcus aureus within the membrane of human polymorphonuclear leukocytes. , 1993, Biochimica et biophysica acta.
[2] A. Brünger,et al. Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement , 1994, Proteins.
[3] P. Couppié,et al. Epidemiological data on Staphylococcus aureus strains producing synergohymenotropic toxins. , 1995, Journal of medical microbiology.
[4] W A Hendrickson,et al. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three‐dimensional structure. , 1990, The EMBO journal.
[5] Y. Kamio,et al. Molecular Biology of the Pore-forming Cytolysins from Staphylococcus aureus, α- and γ-Hemolysins and Leukocidin , 1997 .
[6] J. Gouaux,et al. Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore , 1996, Science.
[7] P. Kraulis. A program to produce both detailed and schematic plots of protein structures , 1991 .
[8] R J Read,et al. [Model phases: probabilities and bias. , 1997, Methods in enzymology.
[9] Y. Kamio,et al. Assembly of Staphylococcus aureus γ‐hemolysin into a pore‐forming ring‐shaped complex on the surface of human erythrocytes , 1997, FEBS letters.
[10] H. Bayley,et al. Molecular architecture of a toxin pore: a 15‐residue sequence lines the transmembrane channel of staphylococcal alpha‐toxin. , 1996, The EMBO journal.
[11] G. Kleywegt,et al. Detecting folding motifs and similarities in protein structures. , 1997, Methods in enzymology.
[12] K. Sharp,et al. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons , 1991, Proteins.
[13] D M Szebenyi,et al. A system for integrated collection and analysis of crystallographic diffraction data. , 1997, Journal of synchrotron radiation.
[14] H. Monteil,et al. The Staphylococcal Pore-forming Leukotoxins Open Ca2+ Channels in the Membrane of Human Polymorphonuclear Neutrophils , 1998, The Journal of Membrane Biology.
[15] E. Gouaux,et al. α‐Hemolysin, γ‐hemolysin, and leukocidin from Staphylococcus aureus: Distant in sequence but similar in structure , 1997 .
[16] H. Bayley,et al. Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin: prototypes of pore-forming bacterial cytolysins , 1996, Archives of Microbiology.
[17] H. Erickson,et al. Crystallization of a fragment of human fibronectin: Introduction of methionine by site‐directed mutagenesis to allow phasing via selenomethionine , 1994, Proteins.
[18] L. Baba-Moussa,et al. A predicted β -sheet from class S components of staphylococcal γ -hemolysin is essential for the secondary interaction of the class F component , 1997 .
[19] L. Lally. The CCP 4 Suite — Computer programs for protein crystallography , 1998 .
[20] H. Hauser,et al. Conformation of phospholipids. Crystal structure of a lysophosphatidylcholine analogue. , 1980, Journal of molecular biology.
[21] H. Bayley,et al. Key Residues for Membrane Binding, Oligomerization, and Pore Forming Activity of Staphylococcal α-Hemolysin Identified by Cysteine Scanning Mutagenesis and Targeted Chemical Modification (*) , 1995, The Journal of Biological Chemistry.
[22] T A Jones,et al. Electron-density map interpretation. , 1997, Methods in enzymology.
[23] Axel T. Brunger,et al. X-PLOR Version 3.1: A System for X-ray Crystallography and NMR , 1992 .
[24] E A Merritt,et al. Raster3D Version 2.0. A program for photorealistic molecular graphics. , 1994, Acta crystallographica. Section D, Biological crystallography.
[25] H. Bayley,et al. Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesis. , 1992, The Journal of biological chemistry.
[26] J. Gouaux,et al. Spontaneous oligomerization of a staphylococcal alpha-hemolysin conformationally constrained by removal of residues that form the transmembrane beta-barrel. , 1997, Protein engineering.
[27] S. Bhakdi,et al. Staphylococcal alpha-toxin: formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages. , 1997, Biochemistry.
[28] P. O’Toole,et al. The gamma-hemolysin locus of Staphylococcus aureus comprises three linked genes, two of which are identical to the genes for the F and S components of leukocidin , 1993, Infection and immunity.
[29] H. Bayley,et al. An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch. , 1995, Chemistry & biology.
[30] E. Gouaux. α-Hemolysin fromStaphylococcus aureus:An Archetype of β-Barrel, Channel-Forming Toxins , 1998 .
[31] Y. Kamio,et al. Molecular cloning and nucleotide sequence of leukocidin F-component gene (lukF) from methicillin resistant Staphylococcus aureus. , 1992, Biochemical and biophysical research communications.
[32] Z. Otwinowski,et al. [20] Processing of X-ray diffraction data collected in oscillation mode. , 1997, Methods in enzymology.
[33] Y. Kamio,et al. Improved method for purification of leukocidin and gamma-hemolysin components from Staphylococcus aureus , 1993 .
[34] David Eisenberg,et al. Unbiased three-dimensional refinement of heavy-atom parameters by correlation of origin-removed Patterson functions , 1983 .
[35] W. Hendrickson. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. , 1991, Science.
[36] G. A. Sim,et al. A note on the heavy‐atom method , 1960 .
[37] H. Bayley,et al. Surface labeling of key residues during assembly of the transmembrane pore formed by staphylococcal α‐hemolysin , 1994, FEBS letters.
[38] D. Kernodle,et al. Site-directed mutagenesis of the alpha-toxin gene of Staphylococcus aureus: role of histidines in toxin activity in vitro and in a murine model , 1994, Infection and immunity.