Structure and function of bacterial outer membrane proteins: barrels in a nutshell
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P. van Gelder | K. Locher | R. Koebnik | Ralf Koebnik | Kaspar P. Locher | Patrick Van Gelder | P. Van Gelder
[1] P. Phale,et al. Brownian dynamics simulation of ion flow through porin channels. , 1999, Journal of molecular biology.
[2] J. Gouaux,et al. Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore , 1996, Science.
[3] C. Ferran,et al. Plasmid-mediated sucrose metabolism in Escherichia coli: characterization of scrY, the structural gene for a phosphoenolpyruvate-dependent sucrose phosphotransferase system outer membrane porin , 1991, Journal of bacteriology.
[4] V. Braun. Energy-coupled transport and signal transduction through the gram-negative outer membrane via TonB-ExbB-ExbD-dependent receptor proteins. , 1995, FEMS microbiology reviews.
[5] V. Braun,et al. Identification of a New Site for Ferrichrome Transport by Comparison of the FhuA Proteins of Escherichia coli,Salmonella paratyphi B, Salmonella typhimurium, and Pantoea agglomerans , 1998, Journal of bacteriology.
[6] G. Rummel,et al. Structural and Functional Characterization of OmpF Porin Mutants Selected for Larger Pore Size , 1996, The Journal of Biological Chemistry.
[7] J. Tommassen,et al. Demonstration of a folded monomeric form of porin PhoE of Escherichia coli in vivo , 1996, Journal of bacteriology.
[8] J. Lakey,et al. Voltage-gating of Escherichia coli porin: a cystine-scanning mutagenesis study of loop 3. , 1998, Journal of molecular biology.
[9] R. Morona,et al. Escherichia coli K-12 outer membrane protein (OmpA) as a bacteriophage receptor: analysis of mutant genes expressing altered proteins , 1984, Journal of bacteriology.
[10] J. Deisenhofer,et al. Crystal structure of the outer membrane active transporter FepA from Escherichia coli , 1999, Nature Structural Biology.
[11] R. Koebnik. In vivo membrane assembly of split variants of the E.coli outer membrane protein OmpA. , 1996, The EMBO journal.
[12] G. Schulz,et al. Refined structure of the porin from Rhodopseudomonas blastica. Comparison with the porin from Rhodobacter capsulatus. , 1994, Journal of molecular biology.
[13] V. Koronakis,et al. Structure of TolC, the outer membrane component of the bacterial type I efflux system, derived from two‐dimensional crystals , 1997, Molecular microbiology.
[14] N. W. Davis,et al. The complete genome sequence of Escherichia coli K-12. , 1997, Science.
[15] M. Karplus,et al. Computer simulations of the OmpF porin from the outer membrane of Escherichia coli. , 1997, Biophysical journal.
[16] V. Braun,et al. The β‐barrel domain of FhuAΔ5‐160 is sufficient for TonB‐dependent FhuA activities of Escherichia coli , 1999, Molecular microbiology.
[17] Scott J. Hultgren,et al. Bacterial Adhesins: Common Themes and Variations in Architecture and Assembly , 1999, Journal of bacteriology.
[18] R. Benz,et al. Pore formation by LamB of Escherichia coli in lipid bilayer membranes , 1986, Journal of bacteriology.
[19] A. Delcour,et al. E.coli PhoE porin has an opposite voltage‐dependence to the homologous OmpF , 1998, The EMBO journal.
[20] Y. Stierhof,et al. An outer membrane protein (OmpA) of Escherichia coli K-12 undergoes a conformational change during export. , 1986, The Journal of biological chemistry.
[21] N. Dekker. Outer‐membrane phospholipase A: known structure, unknown biological function , 2000, Molecular microbiology.
[22] J. Tommassen,et al. Topology of outer membrane pore protein PhoE of Escherichia coli. Identification of cell surface-exposed amino acids with the aid of monoclonal antibodies. , 1986, The Journal of biological chemistry.
[23] R. Liddington,et al. Crystal structure of the anthrax toxin protective antigen , 1997, Nature.
[24] R. Koebnik,et al. Proposal for a peptidoglycan‐associating alpha‐helical motif in the C‐terminal regions of some bacterial cell‐surface proteins , 1995, Molecular microbiology.
[25] H. Engelhardt,et al. Significance of positively charged amino acids for the function of the acidovorax delafieldii porin omp34 , 1995 .
[26] H. Verheij,et al. Inactivation of Escherichia coli outer-membrane phospholipase A by the affinity label hexadecanesulfonyl fluoride. Evidence for an active-site serine. , 1991, European journal of biochemistry.
[27] G. Schulz,et al. Structure of the outer membrane protein A transmembrane domain , 1998, Nature Structural Biology.
[28] J. Rosenbusch,et al. Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution , 1995, Science.
[29] G. Schulz,et al. Energy profile of maltooligosaccharide permeation through maltoporin as derived from the structure and from a statistical analysis of saccharide‐protein interactions , 1997, Protein science : a publication of the Protein Society.
[30] J. Tommassen,et al. Role of the constriction loop in the gating of outer membrane porin PhoE of Escherichia coli , 1997, FEBS letters.
[31] E. Bremer,et al. Single amino acid substitutions affecting the substrate specificity of the Escherichia coli K-12 nucleoside-specific Tsx channel. , 1993, The Journal of biological chemistry.
[32] C. Houssin,et al. Fast and slow kinetics of porin channels from Escherichia coli reconstituted into giant liposomes and studied by patch‐clamp , 1992, FEBS letters.
[33] J. Tommassen,et al. Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein. , 1991, Journal of molecular biology.
[34] Kay Diederichs,et al. Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose , 1998, Nature Structural Biology.
[35] J. Rosenbusch,et al. Voltage sensing in the PhoE and OmpF outer membrane porins of Escherichia coli: role of charged residues. , 1997, Journal of molecular biology.
[36] A. Lesk,et al. Principles determining the structure of beta-sheet barrels in proteins. I. A theoretical analysis. , 1994, Journal of molecular biology.
[37] K. Diederichs,et al. Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. , 1998, Science.
[38] M. A. Payne,et al. Ligand-specific opening of a gated-porin channel in the outer membrane of living bacteria. , 1997, Science.
[39] R. Freudl. Insertion of peptides into cell-surface-exposed areas of the Escherichia coli OmpA protein does not interfere with export and membrane assembly. , 1989, Gene.
[40] L. Regan. Protein Structure: Born to be beta , 1994, Current Biology.
[41] R. Benz,et al. Conversion of the FhuA transport protein into a diffusion channel through the outer membrane of Escherichia coli. , 1993, The EMBO journal.
[42] J. Liu,et al. Formation of a gated channel by a ligand-specific transport protein in the bacterial outer membrane. , 1992, Science.
[43] R. Koebnik,et al. Sugar Transport through Maltoporin of Escherichia coli , 2000, The Journal of Biological Chemistry.
[44] P. Black,et al. Bacterial long-chain fatty acid transport. Identification of amino acid residues within the outer membrane protein FadL required for activity. , 1993, The Journal of biological chemistry.
[45] F. Jähnig,et al. Kinetics of Folding and Membrane Insertion of a β-Barrel Membrane Protein (*) , 1995, The Journal of Biological Chemistry.
[46] Luc Moulinier,et al. Transmembrane Signaling across the Ligand-Gated FhuA Receptor Crystal Structures of Free and Ferrichrome-Bound States Reveal Allosteric Changes , 1998, Cell.
[47] R. Koebnik. Membrane assembly of the Escherichia coli outer membrane protein OmpA: exploring sequence constraints on transmembrane beta-strands. , 1999, Journal of molecular biology.
[48] R. Dutzler,et al. Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. , 1996, Structure.
[49] H. Berendsen,et al. A molecular dynamics study of the pores formed by Escherichia coli OmpF porin in a fully hydrated palmitoyloleoylphosphatidylcholine bilayer. , 1998, Biophysical journal.
[50] S. Cowan,et al. Prediction of membrane‐spanning β‐strands and its application to maltoporin , 1993, Protein science : a publication of the Protein Society.
[51] R. Koebnik,et al. Membrane assembly of circularly permuted variants of the E. coli outer membrane protein OmpA. , 1995, Journal of molecular biology.
[52] Arne Elofsson,et al. Architecture of β‐barrel membrane proteins: Analysis of trimeric porins , 1998 .
[53] J. Vanderleyden,et al. The C‐terminal sequence conservation between OmpA‐related outer membrane proteins and MotB suggests a common function in both Gram‐positive and Gram‐negative bacteria, possibly in the interaction of these domains with peptidoglycan , 1994, Molecular microbiology.
[54] G. Schulz,et al. Molecular architecture and electrostatic properties of a bacterial porin. , 1991, Science.
[55] M. Achtman,et al. Two‐dimensional structure of the Opc invasin from Neisseria meningitidis , 1997, Molecular microbiology.
[56] A. Pugsley. The complete general secretory pathway in gram-negative bacteria. , 1993, Microbiological reviews.
[57] R. Dutzler,et al. Channel specificity: structural basis for sugar discrimination and differential flux rates in maltoporin. , 1997, Journal of molecular biology.
[58] J. Tommassen,et al. Molecular basis of porin selectivity: membrane experiments with OmpC-PhoE and OmpF-PhoE hybrid proteins of Escherichia coli K-12. , 1989, Biochimica et biophysica acta.
[59] J. Tommassen,et al. Pore functioning of outer membrane protein PhoE of Escherichia coli: mutagenesis of the constriction loop L3. , 1997, Protein engineering.
[60] M. Montal. Protein folds in channel structure. , 1996, Current opinion in structural biology.
[61] J. Rosenbusch,et al. Dimerization Regulates the Enzymatic Activity of Escherichia coli Outer Membrane Phospholipase A* , 1997, The Journal of Biological Chemistry.
[62] J. Tommassen,et al. One single lysine residue is responsible for the special interaction between polyphosphate and the outer membrane porin PhoE of Escherichia coli. , 1989, The Journal of biological chemistry.
[63] M. T. Brown,et al. Omptin: an Escherichia coli outer membrane proteinase that activates plasminogen. , 1994, Methods in enzymology.
[64] G. Schulz,et al. The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence. , 1999, Structure.
[65] P. Boulanger,et al. FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5. , 1996, The EMBO journal.
[66] U. Henning,et al. Cell envelope and shape of Escherichia coli: multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins , 1978, Journal of bacteriology.
[67] H. Nikaido,et al. Specificity of diffusion channels produced by lambda phage receptor protein of Escherichia coli. , 1980, Proceedings of the National Academy of Sciences of the United States of America.
[68] J. Tommassen,et al. Escherichia coli outer membrane phospholipase A: role of two serines in enzymatic activity. , 1996, Biochemistry.
[69] A. Delcour. Function and modulation of bacterial porins: insights from electrophysiology. , 1997, FEMS microbiology letters.
[70] N. Orange,et al. Ionophore properties of OmpA of Escherichia coli. , 1993, Biochimica et biophysica acta.
[71] H. Nikaido,et al. Stoichiometry of maltodextrin-binding sites in LamB, an outer membrane protein from Escherichia coli , 1991, Journal of bacteriology.
[72] J. Rosenbusch,et al. Stability of trimeric OmpF porin: the contributions of the latching loop L2. , 1998, Biochemistry.
[73] J. Lengeler,et al. Site-Directed Mutagenesis of Loop L3 of Sucrose Porin ScrY Leads to Changes in Substrate Selectivity , 1999, Journal of bacteriology.
[74] K. H. Kalk,et al. Structural evidence for dimerization-regulated activation of an integral membrane phospholipase , 1999, Nature.
[75] J. Tommassen,et al. Molecular characterization of enterobacterial pldA genes encoding outer membrane phospholipase A , 1994, Journal of bacteriology.
[76] B. Pullman,et al. Membrane Proteins: Structures, Interactions and Models , 1992 .
[77] G. von Heijne,et al. Positively and negatively charged residues have different effects on the position in the membrane of a model transmembrane helix. , 1998, Journal of molecular biology.
[78] P. Phale,et al. Voltage gating of Escherichia coli porin channels: role of the constriction loop. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[79] A. Delcour,et al. The spontaneous gating activity of OmpC porin is affected by mutations of a putative hydrogen bond network or of a salt bridge between the L3 loop and the barrel. , 1998, Protein engineering.
[80] H. Verheij,et al. Inactivation of Escherichia coli outer‐membrane phospholipase A by the affinity label hexadecanesulfonyl fluoride , 1991 .
[81] C. Mannella. The 'ins' and 'outs' of mitochondrial membrane channels. , 1992, Trends in biochemical sciences.
[82] O. Tapia,et al. L3 loop-mediated mechanisms of pore closing in porin: a molecular dynamics perturbation approach. , 1995, Protein engineering.
[83] T. Meyer,et al. Characterization of the Neisseria Iga beta-core. The essential unit for outer membrane targeting and extracellular protein secretion. , 1993, Journal of molecular biology.
[84] M. Hofnung,et al. A cluster of charged and aromatic residues in the C-terminal portion of maltoporin participates in sugar binding and uptake , 1998, Molecular and General Genetics MGG.
[85] Hiroshi Nikaido,et al. OmpA protein of Escherichia coli outer membrane occurs in open and closed channel forms. , 1994, The Journal of biological chemistry.
[86] J. Lakey,et al. Voltage gating is a fundamental feature of porin and toxin β‐barrel membrane channels , 1998, FEBS letters.
[87] G. Schulz,et al. Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside. , 1997, Journal of molecular biology.
[88] L. Dekker,et al. Regulated Binding of the Protein Kinase C Substrate GAP-43 to the V0/C2 Region of Protein Kinase C-δ* , 1997, The Journal of Biological Chemistry.
[89] R. Koebnik. Structural and Functional Roles of the Surface-Exposed Loops of the β-Barrel Membrane Protein OmpA fromEscherichia coli , 1999, Journal of bacteriology.
[90] G. Rummel,et al. Crystal structures explain functional properties of two E. coli porins , 1992, Nature.
[91] J. Lakey,et al. The bacterial porin superfamily: sequence alignment and structure prediction , 1991, Molecular microbiology.
[92] D. Tsernoglou,et al. Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states , 1994, Nature.
[93] J. Fierer,et al. Specificity of the complement resistance and cell association phenotypes encoded by the outer membrane protein genes rck from Salmonella typhimurium and ail from Yersinia enterocolitica , 1994, Infection and immunity.
[94] L. Tamm,et al. Folding intermediates of a beta-barrel membrane protein. Kinetic evidence for a multi-step membrane insertion mechanism. , 1996, Biochemistry.
[95] R. Macnab,et al. The Bacterial Flagellum: Reversible Rotary Propellor and Type III Export Apparatus , 1999, Journal of bacteriology.