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Nature, ISSN 0028-0836, 07/2015, Volume 523, Issue 7562, pp. 555 - 560
Bacteria share their ecological niches with other microbes. The bacterial type VI secretion system is one of the key players in microbial competition, as well... 
INTERBACTERIAL COMPETITION | SYSTEM | AGROBACTERIUM-TUMEFACIENS | SMALL-ANGLE SCATTERING | BACTERIAL TYPE VI | TARGET-CELLS | MULTIDISCIPLINARY SCIENCES | HIGH-RESOLUTION | ICMF FAMILY PROTEIN | ENTEROAGGREGATIVE ESCHERICHIA-COLI | VIBRIO-CHOLERAE | Cytoplasm - chemistry | Protein Structure, Tertiary | Bacterial Secretion Systems | Models, Molecular | Crystallography, X-Ray | Cytoplasm - metabolism | Lipopeptides - biosynthesis | Protein Subunits - biosynthesis | Escherichia coli - chemistry | Microscopy, Electron | Cell Membrane - chemistry | Membrane Proteins - biosynthesis | Multiprotein Complexes - chemistry | Membrane Proteins - chemistry | Multiprotein Complexes - biosynthesis | Periplasm - metabolism | Escherichia coli Proteins - biosynthesis | Escherichia coli - metabolism | Cell Membrane - metabolism | Protein Subunits - chemistry | Lipopeptides - chemistry | Periplasm - chemistry | Porosity | Escherichia coli Proteins - chemistry | Bacterial proteins | Analysis | Cytoplasm | Membrane proteins | Proteins | Polymerization | Membranes | Biosynthesis | Experiments | Bacteriology | Index Medicus | Cell Membrane | Protein Subunits | Multiprotein Complexes | Escherichia coli | Biochemistry, Molecular Biology | Cellular Biology | Membrane Proteins | Life Sciences | Microbiology and Parasitology | Escherichia coli Proteins | Biomolecules | Periplasm | Subcellular Processes | Molecular biology | Lipopeptides
Journal Article
New Phytologist, ISSN 0028-646X, 1/2013, Volume 197, Issue 1, pp. 58 - 64
Journal Article
Science, ISSN 0036-8075, 5/2005, Volume 308, Issue 5726, pp. 1321 - 1323
The protein complement of cellular membranes is notoriously resistant to standard proteomic analysis and structural studies. As a result, membrane proteomes... 
Proteins | Datasets | Child abuse | Escherichia coli | Fluorescence | Reports | Cell membranes | Topology | Proteomes | Modeling | Membrane proteins | GREEN FLUORESCENT PROTEIN | EVOLUTION | EFFLUX | MULTIDRUG TRANSPORTER EMRE | ANGSTROM | MULTIDISCIPLINARY SCIENCES | X-RAY-STRUCTURE | CONDUCTING CHANNEL | SELECTIVITY | PREDICTION | Gene Duplication | Green Fluorescent Proteins - genetics | Escherichia coli Proteins - physiology | Membrane Proteins - analysis | Recombinant Fusion Proteins | Cell Membrane - chemistry | Membrane Proteins - physiology | Cloning, Molecular | Alkaline Phosphatase - analysis | Periplasm - chemistry | Escherichia coli Proteins - analysis | Cytoplasm - chemistry | Genes, Bacterial | Alkaline Phosphatase - genetics | Green Fluorescent Proteins - analysis | Protein Structure, Secondary | Membrane Proteins - genetics | Computational Biology | Proteome | Escherichia coli - chemistry | Membrane Proteins - chemistry | Escherichia coli - genetics | Escherichia coli Proteins - genetics | Escherichia coli Proteins - chemistry | Escherichia coli - ultrastructure | Gene amplification | Physiological aspects | Genetic aspects | Research | Pathogens | Membranes | Bioinformatics | Genomics | Index Medicus | Green Fluorescent Proteins/analysis/genetics | Periplasm/chemistry | Escherichia coli/chemistry/genetics/ultrastructure | Cytoplasm/chemistry | Alkaline Phosphatase/analysis/genetics | Cloning; Molecular | Protein Structure; Secondary | Escherichia coli Proteins/analysis/chemistry/genetics/physiology | Cell Membrane/chemistry | Membrane Proteins/analysis/chemistry/genetics/physiology | Genes; Bacterial
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2015, Volume 290, Issue 34, pp. 20761 - 20773
Complex I (NADH: ubiquinone oxidoreductase) is a multisubunit, membrane-bound enzyme of the respiratory chain. The energy from NADH oxidation in the peripheral... 
3-DIMENSIONAL STRUCTURE | CONSERVED CHARGED RESIDUES | SUBUNIT NUOL | ESCHERICHIA-COLI NDH-1 | ATP SYNTHASE | UBIQUINONE OXIDOREDUCTASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ELECTRON-MICROSCOPY | MEMBRANE DOMAIN | NADH-QUINONE OXIDOREDUCTASE | Protons | Periplasm - enzymology | Molecular Sequence Data | NADH Dehydrogenase - genetics | Structure-Activity Relationship | Electron Transport Complex I - metabolism | NAD - chemistry | Copper - chemistry | Electron Transport Complex I - genetics | Cysteine - metabolism | Periplasm - chemistry | NAD - metabolism | Cytoplasm - chemistry | Protein Structure, Tertiary | Amino Acid Sequence | Cytoplasm - enzymology | Gene Expression | Cross-Linking Reagents - chemistry | Escherichia coli - enzymology | Protein Structure, Secondary | Models, Molecular | Escherichia coli Proteins - metabolism | Cysteine - chemistry | Escherichia coli - chemistry | NADH Dehydrogenase - chemistry | NADH Dehydrogenase - metabolism | Plasmids - metabolism | Electron Transport Complex I - chemistry | Escherichia coli - genetics | Plasmids - chemistry | Escherichia coli Proteins - genetics | Mutation | Escherichia coli Proteins - chemistry | Index Medicus | methanethiosulfonate | proton transport | Bioenergetics | membrane energetics | complex I | membrane protein | cysteine-mediated cross-linking | protein cross-linking
Journal Article
Antimicrobial Agents and Chemotherapy, ISSN 0066-4804, 10/2016, Volume 60, Issue 10, pp. 6013 - 6022
Metallo-beta-lactamases (MBLs) are broad-spectrum, Zn(II)-dependent lactamases able to confer resistance to virtually every beta-lactam antibiotic currently... 
3-DIMENSIONAL STRUCTURE | CHRYSEOBACTERIUM-MENINGOSEPTICUM | ANGSTROM RESOLUTION | MOLECULAR-DYNAMICS | ACTIVE-SITE | PSEUDOMONAS-AERUGINOSA | ESCHERICHIA-COLI | ANTIBIOTIC-RESISTANCE | MICROBIOLOGY | PHARMACOLOGY & PHARMACY | BACILLUS-CEREUS | BINDING-SITES | Flavobacteriaceae - chemistry | Penicillins - chemistry | Periplasm - enzymology | Cephalosporins - chemistry | Glutamine - metabolism | Substrate Specificity | Crystallography, X-Ray | Histidine - metabolism | Zinc - chemistry | beta-Lactamases - genetics | Carbapenems - chemistry | Penicillins - metabolism | Anti-Bacterial Agents - chemistry | Drug Resistance, Multiple, Bacterial | Cloning, Molecular | Escherichia coli - metabolism | Protein Domains | Glutamine - chemistry | Periplasm - chemistry | beta-Lactamases - metabolism | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Carbapenems - metabolism | Protein Conformation, alpha-Helical | Catalytic Domain | Gene Expression | Recombinant Proteins - chemistry | Anti-Bacterial Agents - metabolism | Flavobacteriaceae - enzymology | Recombinant Proteins - genetics | Molecular Dynamics Simulation | beta-Lactamases - chemistry | Cations, Divalent | Protein Conformation, beta-Strand | Escherichia coli - genetics | Protein Binding | Molecular Docking Simulation | Kinetics | Histidine - chemistry | Cephalosporins - metabolism | Index Medicus | Life Sciences
Journal Article
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 12/2017, Volume 85, Issue 12, pp. 2217 - 2230
Periplasmic heme‐binding proteins (PBPs) in Gram‐negative bacteria are components of the heme acquisition system. These proteins shuttle heme across the... 
iron | X‐ray crystallography | resonance Raman spectroscopy | X-ray crystallography | PROTEIN | TRANSPORTERS | CRYSTAL-STRUCTURE | HASA | BIOCHEMISTRY & MOLECULAR BIOLOGY | CRYSTALLOGRAPHY | SOFTWARE | NEAT DOMAIN | BIOPHYSICS | YERSINIA-PESTIS | STAPHYLOCOCCUS-AUREUS | PATHOGENS | Burkholderia cenocepacia - chemistry | Heme - metabolism | Chloroflexi - chemistry | Crystallography, X-Ray | Heme - chemistry | Periplasm - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Protein Interaction Domains and Motifs | Periplasm - chemistry | Binding Sites | Periplasmic Binding Proteins - genetics | Tyrosine - chemistry | Periplasmic Binding Proteins - metabolism | Periplasmic Binding Proteins - chemistry | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Iron - chemistry | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Iron - metabolism | Plasmids - metabolism | Amino Acid Motifs | Arginine - chemistry | Tyrosine - metabolism | Hydrogen Bonding | Protein Conformation, beta-Strand | Burkholderia cenocepacia - metabolism | Escherichia coli - genetics | Plasmids - chemistry | Hydrophobic and Hydrophilic Interactions | Protein Binding | Chloroflexi - metabolism | Arginine - metabolism | Proteins | Analysis | Binding | Translocation | Titration calorimetry | Iron | Hydrophobicity | Hydrogen bonding | Receptors | Conserved sequence | Hydrogen bonds | Spacecraft components | Periplasmic space | Heme | Calorimetry | Bacteria | Titration | Gram-negative bacteria | Burkholderia | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 10/2015, Volume 290, Issue 44, pp. 26675 - 26687
TolR is a 15-kDa inner membrane protein subunit of the Tol-Pal complex in Gram-negative bacteria, and its function is poorly understood. Tol-Pal is recruited... 
PEPTIDOGLYCAN RECOGNITION | ORGANIZATION | KEY RESIDUES | COMPLEX | CONFORMATIONAL-CHANGE | TERMINAL DOMAIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | FORCE-FIELD | BACTERIAL FLAGELLAR MOTOR | SECONDARY STRUCTURE | SIMULATIONS | Peptidoglycan - metabolism | Lipoproteins - genetics | Peptidoglycan - chemistry | Protein Multimerization | Bacterial Proteins - chemistry | Molecular Sequence Data | Crystallography, X-Ray | Periplasm - metabolism | Flagella - chemistry | Escherichia coli - metabolism | Lipoproteins - metabolism | Membrane Proteins - metabolism | Periplasm - chemistry | Binding Sites | Bacterial Outer Membrane Proteins - genetics | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Gene Expression | Protein Structure, Secondary | Membrane Proteins - genetics | Bacterial Proteins - genetics | Bacterial Outer Membrane Proteins - chemistry | Models, Molecular | Recombinant Proteins - chemistry | Escherichia coli Proteins - metabolism | Lipoproteins - chemistry | Peptidoglycan - genetics | Recombinant Proteins - genetics | Escherichia coli - chemistry | Sequence Alignment | Flagella - metabolism | Bacterial Outer Membrane Proteins - metabolism | Membrane Proteins - chemistry | Escherichia coli Proteins - genetics | Hydrophobic and Hydrophilic Interactions | Protein Binding | Bacterial Proteins - metabolism | Escherichia coli Proteins - chemistry | Index Medicus | Protein Structure and Folding | bacteria | periplasm | Escherichia coli (E. coli) | TolR | domain | crystal structure | dimerization | membrane protein | strand-swapped
Journal Article
Nature, ISSN 0028-0836, 09/2017, Volume 549, Issue 7671, pp. 233 - 237
Lipopolysaccharide (LPS) in the outer membrane of Gram-negative bacteria is critical for the assembly of their cell envelopes. LPS synthesized in the... 
BINDING CASSETTE TRANSPORTER | ABC TRANSPORTER | MOLECULAR-MECHANISM | COMPLEX | RECOGNITION | RESONANCE | BIOSYNTHESIS | MULTIDISCIPLINARY SCIENCES | ALTERNATING ACCESS | DIVERSITY | FLIPPASE | Bacterial Proteins - chemistry | Lipopolysaccharides - metabolism | Adenosine Diphosphate - chemistry | Escherichia coli - cytology | Cell Membrane - chemistry | ATP-Binding Cassette Transporters - chemistry | Biological Transport | Periplasm - metabolism | ATP-Binding Cassette Transporters - metabolism | Protein Domains | Cell Membrane - metabolism | Periplasm - chemistry | Periplasm - ultrastructure | Nanostructures - ultrastructure | Escherichia coli - enzymology | Models, Molecular | Cell Membrane - ultrastructure | Cryoelectron Microscopy | ATP-Binding Cassette Transporters - ultrastructure | Hydrophobic and Hydrophilic Interactions | Nanostructures - chemistry | Protein Binding | Bacterial Proteins - metabolism | Bacterial Proteins - ultrastructure | Adenosine Diphosphate - metabolism | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Escherichia coli - ultrastructure | Biological research | Biological transport | Physiological aspects | Cell membranes | Research | Lipopolysaccharides | Biology, Experimental | Lipids | Hydrophobicity | Electron microscopy | ADP | Vanadate | Proteins | Transmission electron microscopy | Bacteria | Transmembrane domains | Gram-negative bacteria | Embedded structures | Cell envelopes | Transporter | Adenosine triphosphate | Conformation | Structural analysis | Index Medicus
Journal Article
Biophysical Journal, ISSN 0006-3495, 2009, Volume 97, Issue 8, pp. 2250 - 2257
The oligo-acyl-lysyl, C K- , is comprised of only three Lys residues. Despite its small size, it exhibits potent bacteriostatic activity against Gram-positive... 
BIOPHYSICS | MECHANISM | LYSINE OLIGOMERS | ESCHERICHIA-COLI | MODE | LIPOPOLYSACCHARIDE | DEFENSINS | ANTIMICROBIAL PEPTIDES | Escherichia coli - drug effects | Peptidoglycan - chemistry | DNA, Bacterial - chemistry | Teichoic Acids - chemistry | Periplasm - drug effects | Cell Membrane - chemistry | Dose-Response Relationship, Drug | Cell Wall - drug effects | Anti-Bacterial Agents - chemistry | Edetic Acid - pharmacology | Periplasm - chemistry | Cell Membrane - drug effects | Dipeptides - pharmacology | Chelating Agents - chemistry | Membranes, Artificial | Cell Wall - chemistry | Chelating Agents - pharmacology | Permeability | Dipeptides - chemistry | Escherichia coli - chemistry | Static Electricity | Staphylococcus aureus - chemistry | Edetic Acid - chemistry | Models, Biological | Peptidoglycan - drug effects | Anti-Bacterial Agents - pharmacology | Lipopolysaccharides - chemistry | Staphylococcus aureus - drug effects | Bacteria | Membranes | Biophysics | Cells | Deoxyribonucleic acid--DNA | Index Medicus | Binding | Lipids | Position (location) | Adhesion | Electrostatics | Walls | Contact | CAC, critical aggregation concentration | DSC, differential scanning calorimetry | ONPG, ortho-nitrophenyl-β-D-galactoside | ITC, isothermal titration calorimetry | LTA, lipoteichoic acid | CL, cardiolipin | ANTS, 8-aminonaphthalene-1,3,6-trisulfonic acid | PE, phosphatidylethanolamine | DOPG, dioleoyl phosphatidylglycerol | OAK, oligo-acyl-lysyl | MIC, minimal inhibitory concentration | TOCL, tetraoleoyl cardiolipin | LUV, large unilamellar vesicle | PG, phosphatidylglycerol | POPE, 1-palmitoyl-2-oleoylphosphatidylethanolamine | PBS, phosphate-buffered saline | DPX, p-xylene-bis-pyridinium bromide | LB, Luria-Bertani broth | TSB, tryptic soy broth | CFU, colony-forming unit | Membrane | LPS, lipopolysaccharide | ONP, ortho-nitrophenyl | SPR, surface plasmon resonance
Journal Article
PLoS ONE, ISSN 1932-6203, 02/2017, Volume 12, Issue 2, pp. e0172823 - e0172823
Journal Article