Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Combined Automated Annotation using Multiple IEA Methods
Penicillin-binding proteins and cell shape in E. coli.
Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.
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Foundational study identifying PBP2 as essential for rod shape
"The varied effects of beta-lactam antibiotics on cell division, cell elongation, and cell shape in E. coli are shown to be due to the presence of three essential penicillin binding proteins"
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Mutants failing to bind beta-lactams to PBP2 grow as round cells
"A mutant has been isolated that fails to bind beta-lactams to protein 2, and that grows as round cells"
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PBP2 is associated with cell elongation
"beta-Lactams that specifically result in the production of ovoid cells bind to penicillin binding protein 2"
Constitutive septal murein synthesis in Escherichia coli with impaired activity of the morphogenetic proteins RodA and penicillin-binding protein 2.
Active-site residues of the transpeptidase domain of penicillin-binding protein 2 from Escherichia coli: similarity in catalytic mechanism to class A beta-lactamases.
Growth of Escherichia coli: significance of peptidoglycan degradation during elongation and septation.
Cooperativity of peptidoglycan synthases active in bacterial cell elongation.
RodZ links MreB to cell wall synthesis to mediate MreB rotation and robust morphogenesis.
Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillin-binding protein 2 and rodA protein.
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Demonstrated PBP2/RodA-dependent peptidoglycan synthesis
"The cross-linked peptidoglycan was synthesized from UDP-N-acetylmuramylpentapeptide and UDP-N-acetylglucosamine"
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Cross-linking activity inhibited by mecillinam
"The cross-linking reaction was strongly inhibited by the amidinopenicillin, mecillinam"
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Required both PBP2 and RodA for peptidoglycan formation
"The formation of peptidoglycan required the presence of high levels of both PBP-2 and the RodA protein"
Structural Basis for E. coli Penicillin Binding Protein (PBP) 2 Inhibition, a Platform for Drug Design.
Identification of the penicillin-binding active site of penicillin-binding protein 2 of Escherichia coli.
RodZ: a key-player in cell elongation and cell division in Escherichia coli.
MreC and MreD balance the interaction between the elongasome proteins PBP2 and RodA.
Nucleotide sequence of the pbpA gene and characteristics of the deduced amino acid sequence of penicillin-binding protein 2 of Escherichia coli K12.
Structural basis of peptidoglycan synthesis by E. coli RodA-PBP2 complex.
Cell shape and division in Escherichia coli: experiments with shape and division mutants.
Cluster of mrdA and mrdB genes responsible for the rod shape and mecillinam sensitivity of Escherichia coli.
A mecillinam-sensitive peptidoglycan crosslinking reaction in Escherichia coli.
Affinity chromatography as a means to study multienzyme complexes involved in murein synthesis.
Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli.
Deep research on E. coli mrdA/PBP2
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PBP2 is a D,D-transpeptidase
"PBP2 is a D,D-transpeptidase that forms 4->3 peptide crosslinks"
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PBP2 is an inner membrane protein
"PBP2 is an inner-membrane bitopic protein with a large periplasmic catalytic domain"
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PBP2 forms complex with RodA
"It forms the RodA-PBP2 complex"