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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 | Membrane proteins | Streptococcus infections | Proteins | Domains | Synthesis | Listeria | Scaffolding | Penicillin | Cell cycle | Bacteria | Viability
Journal Article
FEMS Microbiology Reviews, ISSN 0168-6445, 03/2008, Volume 32, Issue 2, pp. 234 - 258
Penicillin‐binding proteins (PBPs) have been scrutinized for over 40 years. Recent structural information on PBPs together with the ongoing long‐term... 
3D structure | transpeptidase | penicillin‐binding | transglycosylase | peptidoglycan synthesis | Peptidoglycan synthesis | Transglycosylase | Penicillin-binding | Transpeptidase | BETA-LACTAM RESISTANCE | ACYL-ENZYME COMPLEX | ESCHERICHIA-COLI | penicillin-binding | ALA-PEPTIDASE REVEALS | MICROBIOLOGY | PREDICTED SECONDARY STRUCTURES | ENTEROCOCCUS-FAECIUM BM4339 | STREPTOCOCCUS-PNEUMONIAE | BACILLUS-SUBTILIS | ALANINE CARBOXYPEPTIDASE IA | CELL-WALL PEPTIDOGLYCAN | Protein Structure, Tertiary | Bacteria - metabolism | Peptidyl Transferases - metabolism | Bacteria - chemistry | Multienzyme Complexes - classification | Peptidoglycan Glycosyltransferase - metabolism | Peptidoglycan Glycosyltransferase - chemistry | Glycosyltransferases - chemistry | Penicillin-Binding Proteins - classification | Peptidyl Transferases - chemistry | Bacterial Proteins - chemistry | Multienzyme Complexes - metabolism | Penicillin-Binding Proteins - metabolism | Peptide Hydrolases - chemistry | Multienzyme Complexes - chemistry | Peptidoglycan - biosynthesis | Glycosyltransferases - metabolism | beta-Lactams - pharmacology | Penicillin-Binding Proteins - chemistry | Bacterial Proteins - metabolism | Bacterial Proteins - classification | beta-Lactamases - metabolism | Peptide Hydrolases - metabolism | Physiological aspects | Peptidoglycans
Journal Article
Science, ISSN 0036-8075, 7/2011, Volume 333, Issue 6039, pp. 225 - 228
Journal Article
ANNUAL REVIEW OF BIOCHEMISTRY, ISSN 0066-4154, 2008, Volume 77, pp. 383 - 414
Genome sequencing projects have provided researchers with a complete inventory of the predicted proteins produced by eukaryotic and prokaryotic organisms.... 
NUCLEOTIDE LIPOPHILIC PRODRUGS | proteomics | ACTIVITY-BASED PROTEOMICS | BREAST-CANCER METASTASIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | KINASE INHIBITORS | PENICILLIN-BINDING COMPONENTS | COMPLEX PROTEOMES | ACTIVITY-BASED PROBES | affinity label | ACID AMIDE HYDROLASE | IN-VIVO | mass spectrometry | FUNCTIONAL PROTEOMICS
Journal Article
The FEBS Journal, ISSN 1742-464X, 01/2018, Volume 285, Issue 1, pp. 87 - 100
The β‐lactam antibiotics inhibit penicillin‐binding proteins (PBPs) by forming a stable, covalent, acyl‐enzyme complex. During the evolution from PBPs to Class... 
penilloate | penicillin‐binding protein | X‐ray crystallography | CTX‐M | penicilloate | CTX-M | X-ray crystallography | penicillin-binding protein | MYCOBACTERIUM-TUBERCULOSIS | ACYL-ENZYME | MOLECULAR-STRUCTURE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | ANTIBIOTIC-RESISTANCE | ACYLATION MECHANISM | ANGSTROM RESOLUTION | PENICILLIN-BINDING PROTEINS | Protons | Crystallography, X-Ray | Penicillin-Binding Proteins - genetics | Penicillanic Acid - chemistry | Penicillin-Binding Proteins - chemistry | beta-Lactamases - genetics | beta-Lactamases - metabolism | Penicillanic Acid - analogs & derivatives | Recombinant Proteins - metabolism | Biocatalysis | Mutant Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Mutant Proteins - metabolism | Recombinant Proteins - genetics | Binding Sites - genetics | Penicillin-Binding Proteins - metabolism | Penicillanic Acid - metabolism | beta-Lactamases - chemistry | Hydrogen Bonding | Organometallic Compounds - metabolism | Escherichia coli - genetics | Mutant Proteins - chemistry | Organometallic Compounds - chemistry | Protein Conformation | Amino Acid Substitution | Enzymes | β-Lactam antibiotics | Product inhibition | Serine | Amides | Nitrogen | Hydrogen bonding | Data bases | Proteins | Databases | Antibiotics | Lysine | Penicillin | Protonation | Catalysis | Coordination compounds | Bonding | Crystal structure | Penilloate | Penicillin Binding Protein | Penicilloate | BASIC BIOLOGICAL SCIENCES | Penicillin-Binding Protein
Journal Article
Microbial Drug Resistance, ISSN 1076-6294, 09/2016, Volume 22, Issue 6, pp. 446 - 460
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
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... 
BETA-LACTAM RESISTANCE | CELL-DIVISION | LOCALIZATION | COMPLEX | MECHANISM | LYTIC TRANSGLYCOSYLASE | MULTIDISCIPLINARY SCIENCES | MACHINERY | GLOBULAR-PROTEINS | MEMBRANE-PROTEINS | INHIBITOR | 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
ChemBioChem, ISSN 1439-4227, 12/2016, Volume 17, Issue 23, pp. 2250 - 2256
Journal Article
Nature, ISSN 0028-0836, 08/2016, Volume 537, Issue 7622, pp. 634 - 638
Journal Article