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Found 3 records.
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1. (CSDB ID: 1129) | report error |
| EtN-(1--P--6)--+ | -4)-b-D-Glcp-(1-4)-b-D-Glcp-(1- | Show graphically |
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Escherichia coli K-12 W3110
(NCBI TaxID 316407,
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Escherichia coli K-12 AR3110
(Ancestor NCBI TaxID 83333,
species name lookup)
Escherichia coli O18:K1:H7 UTI89
(Ancestor NCBI TaxID 1095706,
species name lookup)
]; hemolytic-uremic syndrome (HUS) [ICD11: 3A21.2 ]; infection due to Escherichia coli [ICD11: XN6P4 ]
stanford.edu; regine.henggehu-berlin.deCellulose is a major contributor to the chemical and mechanical properties of plants and assumes structural roles in bacterial communities termed biofilms. We find that Escherichia coli produces chemically modified cellulose that is required for extracellular matrix assembly and biofilm architecture. Solid-state nuclear magnetic resonance spectroscopy of the intact and insoluble material elucidates the zwitterionic phosphoethanolamine modification that had evaded detection by conventional methods. Installation of the phosphoethanolamine group requires BcsG, a proposed phosphoethanolamine transferase, with biofilm-promoting cyclic diguanylate monophosphate input through a BcsE-BcsF-BcsG transmembrane signaling pathway. The bcsEFG operon is present in many bacteria, including Salmonella species, that also produce the modified cellulose. The discovery of phosphoethanolamine cellulose and the genetic and molecular basis for its production offers opportunities to modulate its production in bacteria and inspires efforts to biosynthetically engineer alternatively modified cellulosic materials
biosynthesis, genetic, Escherichia coli, Biofilm, cellulose, transmembrane, phosphoethanolamine transferase
Structure type: fragment of a bigger structure|
2. (CSDB ID: 23702) | report error |
| a-D-Glcp-(1-2)-+ D-Ala-(1-2)-+ | | {{{-D-Gro-(1--P--3)--}}}D-Gro-(1--P--3)--D-Gro-(1--P--3)--D-Gro-(1--P--6)--a-D-Glcp-(1-6)-a-D-Glcp-(1---P---/peptidoglycan/ | Show graphically |
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Bacillus subtilis
(NCBI TaxID 1423,
species name lookup)
]ou.eduThe conformation of d-alanine (d-Ala) groups of bacterial teichoic acid is a central, yet untested, paradigm of microbiology. The d-Ala binds via the C-terminus, thereby allowing the amine to exist as a free cationic NH(3)(+) group with the ability to form a contact ion pair with the nearby anionic phosphate group. This conformation hinders metal chelation by the phosphate because the zwitterion pair is charge neutral. To the contrary, the repulsion of cationic antimicrobial peptides (CAMPs) is attributed to the presence of the d-Ala cation; thus the ion pair does not form in this model. Solid-state nuclear magnetic resonance (NMR) spectroscopy has been used to measure the distance between amine and phosphate groups within cell wall fragments of Bacillus subtilis. The bacteria were grown on media containing (15)N d-Ala and β-chloroalanine racemase inhibitor. The rotational-echo double-resonance (REDOR) pulse sequence was used to measure the internuclear dipolar coupling, and the results demonstrate (1) the metal-free amine-to-phosphate distance is 4.4 A and (2) the amine-to-phosphate distance increases to 5.4 A in the presence of Mg(2+) ions. As a result, the zwitterion exists in a nitrogen-oxygen ion pair configuration providing teichoic acid with a positive charge to repel CAMPs. Additionally, the amine of d-Ala does not prevent magnesium chelation in contradiction to the prevailing view of teichoic acids in metal binding. Thus, the NMR-based description of teichoic acid structure resolves the contradictory models, advances the basic understanding of cell wall biochemistry, and provides possible insight into the creation of new antibiotic therapies
NMR, conformation, lipopolysaccharides, structure, chemistry, Bacterial, metabolism, microbiology, cell, group, ion, form, solid state, acid, phosphate, bacteria, neutral, cell wall, chemical, biochemistry, Magnetic Resonance Spectroscopy, nuclear, nuclear magnetic resonance, nuclear magnetic resonance spectroscopy, resonance, spectroscopy, sequence, teichoic acids, fragment, Carbohydrate Conformation, binding, teichoic acid, peptides, ability, peptidoglycan, Bacillus, phosphorus, Acids, model, models, Alanine, Bacillus subtilis, configuration, free, medium, distance, therapy, coupling, dipolar coupling, peptide, Magnesium, anionic, phospholipids, inhibitor, cation, antibiotic, antimicrobial, cationic, Binding Sites, Phosphates, D-alanine, amine, Anions, antibiotic therapy, charge, Chelating Agents, Ions, metal, metal-binding, pulse, pulse sequence
Structure type: oligomer|
3. (CSDB ID: 23999) | report error |
| a-D-GlcpNAc-(1-2)-+ D-Ala-(1-2)-+ | | {{{-D-Gro-(1--P--3)--}}}D-Gro-(1--P--3)--D-Gro-(1--P--3)--D-Gro-(1--P--6)--a-D-Glcp-(1-6)-a-D-Glcp-(1-?)-LIP | Show graphically |
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Bacillus subtilis
(NCBI TaxID 1423,
species name lookup)
]ou.eduThe conformation of d-alanine (d-Ala) groups of bacterial teichoic acid is a central, yet untested, paradigm of microbiology. The d-Ala binds via the C-terminus, thereby allowing the amine to exist as a free cationic NH(3)(+) group with the ability to form a contact ion pair with the nearby anionic phosphate group. This conformation hinders metal chelation by the phosphate because the zwitterion pair is charge neutral. To the contrary, the repulsion of cationic antimicrobial peptides (CAMPs) is attributed to the presence of the d-Ala cation; thus the ion pair does not form in this model. Solid-state nuclear magnetic resonance (NMR) spectroscopy has been used to measure the distance between amine and phosphate groups within cell wall fragments of Bacillus subtilis. The bacteria were grown on media containing (15)N d-Ala and β-chloroalanine racemase inhibitor. The rotational-echo double-resonance (REDOR) pulse sequence was used to measure the internuclear dipolar coupling, and the results demonstrate (1) the metal-free amine-to-phosphate distance is 4.4 A and (2) the amine-to-phosphate distance increases to 5.4 A in the presence of Mg(2+) ions. As a result, the zwitterion exists in a nitrogen-oxygen ion pair configuration providing teichoic acid with a positive charge to repel CAMPs. Additionally, the amine of d-Ala does not prevent magnesium chelation in contradiction to the prevailing view of teichoic acids in metal binding. Thus, the NMR-based description of teichoic acid structure resolves the contradictory models, advances the basic understanding of cell wall biochemistry, and provides possible insight into the creation of new antibiotic therapies
NMR, conformation, lipopolysaccharides, structure, chemistry, Bacterial, metabolism, microbiology, cell, group, ion, form, solid state, acid, phosphate, bacteria, neutral, cell wall, chemical, biochemistry, Magnetic Resonance Spectroscopy, nuclear, nuclear magnetic resonance, nuclear magnetic resonance spectroscopy, resonance, spectroscopy, sequence, teichoic acids, fragment, Carbohydrate Conformation, binding, teichoic acid, peptides, ability, peptidoglycan, Bacillus, phosphorus, Acids, model, models, Alanine, Bacillus subtilis, configuration, free, medium, distance, therapy, coupling, dipolar coupling, peptide, Magnesium, anionic, phospholipids, inhibitor, cation, antibiotic, antimicrobial, cationic, Binding Sites, Phosphates, D-alanine, amine, Anions, antibiotic therapy, charge, Chelating Agents, Ions, metal, metal-binding, pulse, pulse sequence
Structure type: oligomer| New query | Export IDs | Home | Help |
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