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Literature summary for 3.4.16.4 extracted from

  • Meiresonne, N.; van der Ploeg, R.; Hink, M.; den Blaauwen, T.
    Activity-related conformational changes in D,D-carboxypeptidases revealed by in vivo periplasmic Foerster resonance energy transfer assay in Escherichia coli (2017), mBio, 8, e01089 .
    View publication on PubMedView publication on EuropePMC
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Application

Application Comment Organism
analysis Forster resonance energy transfer assay that uses the fluorescent-protein donor-acceptor pair mNeonGreen-mCherry to detect periplasmic protein interactions in fixed and in living bacteria, in single samples or in plate reader 96-well format Escherichia coli

Protein Variants

Protein Variants Comment Organism
S44G active site mutant, isoform PBP5, inactive, mutation changes the conformation of the dimeric state. Contrary to wild-type, the mutant only localized laterally in the cell Escherichia coli
S63G active site mutant, isoform PBP6b, inactive, mutation changes the conformation of the dimeric state Escherichia coli
S66G active site mutant, isoform PBP6a, inactive, mutation changes the conformation of the dimeric state. Contrary to wild-type, the mutant mostly avoids midcell localization Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information in minimal-medium-grown cells, wild-type PBP5 localizes laterally and at the midcell. Isoform PBP6a localization is lateral and intense at the midcell. PBP6b localizes poorly at the midcell and mainly at the lateral sides Escherichia coli
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Synonyms

Synonyms Comment Organism
PBP5
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 Escherichia coli
PBP6a
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 Escherichia coli
PBP6b
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 Escherichia coli

General Information

General Information Comment Organism
physiological function D,D-CPases PBP5, PBP6a, and PBP6b change dimer conformation between resting and active states. The isoforms are not redundant but that their balanced activity is required for robust peptidoglycan synthesis Escherichia coli