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Science, ISSN 0036-8075, 7/2011, Volume 333, Issue 6039, pp. 225 - 228
Journal Article
Nature Communications, ISSN 2041-1723, 12/2019, Volume 10, Issue 1, pp. 261 - 17
Bacterial growth and cell division requires precise spatiotemporal regulation of the synthesis and remodelling of the peptidoglycan layer that surrounds the... 
MINICELL LOCUS | STREPTOCOCCUS-PNEUMONIAE | FTSZ | MULTIDISCIPLINARY SCIENCES | GROWTH | PENICILLIN-BINDING PROTEIN | COMPONENT | IDENTIFICATION | PEPTIDOGLYCAN SYNTHESIS | DIVISION | REQUIREMENT | Virulence Factors - genetics | Bacterial Proteins - chemistry | Crystallography, X-Ray | Penicillin-Binding Proteins - genetics | Protein Interaction Maps | Cell Cycle Proteins - chemistry | Recombinant Proteins - isolation & purification | Penicillin-Binding Proteins - chemistry | Streptococcus pneumoniae - metabolism | Cell Division | Cell Cycle Proteins - genetics | Listeria monocytogenes - metabolism | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Recombinant Proteins - metabolism | Cell Cycle Proteins - isolation & purification | Bacterial Proteins - genetics | Cell Cycle Proteins - metabolism | Recombinant Proteins - chemistry | Virulence Factors - isolation & purification | Recombinant Proteins - genetics | Virulence Factors - chemistry | Penicillin-Binding Proteins - metabolism | Amino Acid Motifs | Peptidoglycan - biosynthesis | Penicillin-Binding Proteins - isolation & purification | Mutagenesis | Cell Wall - metabolism | Bacterial Proteins - metabolism | Cytosol - metabolism | Virulence Factors - metabolism | Bacterial Proteins - isolation & purification | Bacillus subtilis - metabolism | Enzymes | Cell walls | Peptidoglycans | Cell division | Listeria monocytogenes | Membrane proteins | Streptococcus infections | Proteins | Domains | Synthesis | Listeria | Scaffolding | Penicillin | Cell cycle | Bacteria | Viability
Journal Article
PLoS ONE, ISSN 1932-6203, 05/2014, Volume 9, Issue 5, p. e98042
In Escherichia coli, penicillin-binding protein 3 (PBP3), also known as FtsI, is a central component of the divisome, catalyzing cross-linking of the cell wall... 
FORMS | BETA-LACTAM RESISTANCE | CELL-DIVISION | COMPLEX | MECHANISM | LYTIC TRANSGLYCOSYLASE | MULTIDISCIPLINARY SCIENCES | FTSN | GLOBULAR-PROTEINS | RESISTANT STAPHYLOCOCCUS-AUREUS | MEMBRANE-PROTEINS | Catalytic Domain | Peptidoglycan Glycosyltransferase - metabolism | Peptidoglycan Glycosyltransferase - chemistry | Peptidoglycan Glycosyltransferase - isolation & purification | Protein Multimerization | Models, Molecular | Escherichia coli Proteins - metabolism | Penicillin-Binding Proteins - genetics | Penicillin-Binding Proteins - metabolism | Escherichia coli Proteins - isolation & purification | Peptidoglycan Glycosyltransferase - genetics | Penicillin-Binding Proteins - chemistry | Penicillin-Binding Proteins - isolation & purification | Escherichia coli - genetics | Escherichia coli - metabolism | Escherichia coli Proteins - genetics | Protein Binding | Protein Conformation | Protein Interaction Domains and Motifs | Escherichia coli Proteins - chemistry | Chemical properties | Structure | Escherichia coli | Crystals | Protein binding | Penicillin-binding protein | Peptides | Cell walls | Peptidoglycans | Cell division | Staphylococcus infections | Crosslinking | Biochemistry | Molecular weight | Penicillin-binding protein 3 | E coli | Antibiotics | Penicillin | Bacteria | Electron density | Dimerization | Protein structure | Crystal structure
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2009, Volume 106, Issue 22, pp. 8824 - 8829
Drug-resistant bacteria have caused serious medical problems in recent years, and the need for new antibacterial agents is undisputed. Transglycosylase, a... 
Proteins | Antibiotics | Molecular structure | Cell walls | Drug interactions | Escherichia coli | Crystals | Lipids | Bacteria | Crystal structure | Peptidoglycan synthesis | Membrane protein structure | Protein-protein interaction | Antibacterial development | Antibiotic resistance | ANTIBIOTICS | DESIGN | DOMAIN | LYTIC TRANSGLYCOSYLASE | PROTEIN-STRUCTURE | MULTIDISCIPLINARY SCIENCES | MODEL | membrane protein structure | antibacterial development | REPAIR | antibiotic resistance | MOENOMYCIN | protein-protein interaction | BINDING | CELL-WALL PEPTIDOGLYCAN | peptidoglycan synthesis | Amino Acid Sequence | Escherichia coli - enzymology | Peptidoglycan Glycosyltransferase - chemistry | Molecular Sequence Data | Crystallography, X-Ray | Serine-Type D-Ala-D-Ala Carboxypeptidase - chemistry | Penicillin-Binding Proteins - chemistry | Serine-Type D-Ala-D-Ala Carboxypeptidase - antagonists & inhibitors | Enzyme Inhibitors - chemistry | Oligosaccharides - chemistry | Protein Conformation | Peptidoglycan Glycosyltransferase - antagonists & inhibitors | Escherichia coli Proteins - antagonists & inhibitors | Penicillin-Binding Proteins - antagonists & inhibitors | Escherichia coli Proteins - chemistry | Physiological aspects | Properties | Bacterial proteins | Membrane proteins | Ionizing radiation | Enzymatic activity | Drug resistance | Protein interaction | Antibacterial agents | penicillin-binding protein 1b | moenomycin | Biological Sciences | Physical Sciences | protein–protein interaction
Journal Article
Molecular Microbiology, ISSN 0950-382X, 05/2008, Volume 68, Issue 3, pp. 720 - 735
Journal Article
Molecular Microbiology, ISSN 0950-382X, 07/2006, Volume 61, Issue 1, pp. 33 - 45
In order to divide, the bacterium Escherichia coli must assemble a set of at least 10 essential proteins at the nascent division site. These proteins localize... 
LOCALIZATION | SITE | BACILLUS-SUBTILIS | LYTIC TRANSGLYCOSYLASE | MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI FTSZ | BINDING-PROTEIN | MICROBIOLOGY | SEPTAL RING | STAPHYLOCOCCUS-AUREUS | ZIPA | Penicillin-Binding Proteins - physiology | Multiprotein Complexes - genetics | Penicillin-Binding Proteins - genetics | Escherichia coli - cytology | Escherichia coli Proteins - physiology | Recombinant Fusion Proteins - metabolism | Multiprotein Complexes - metabolism | Membrane Proteins - physiology | Peptidoglycan Glycosyltransferase - physiology | Cell Cycle Proteins - genetics | Membrane Proteins - metabolism | Escherichia coli - physiology | Cell Division - genetics | Peptidoglycan Glycosyltransferase - metabolism | Membrane Proteins - genetics | Bacterial Proteins - genetics | Cell Cycle Proteins - metabolism | Escherichia coli Proteins - metabolism | Penicillin-Binding Proteins - metabolism | Bacterial Proteins - physiology | Multiprotein Complexes - physiology | Cell Division - physiology | Peptidoglycan Glycosyltransferase - genetics | Escherichia coli - genetics | Models, Biological | Escherichia coli Proteins - genetics | Protein Binding | Recombinant Fusion Proteins - genetics | Bacterial Proteins - metabolism | Cell Cycle Proteins - physiology | Microscopy, Fluorescence | Proteins | Cell division | Escherichia coli
Journal Article
PLoS ONE, ISSN 1932-6203, 09/2013, Volume 8, Issue 9, p. e75522
Journal Article
Journal Article
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