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Probing the mechanism of peptidoglycan amidase activation by FtsEX-EnvC
by
Cook, Jonathan
, Crow, Allister
in
ABC transporter
/ ABC transporters
/ Amidase
/ Amidohydrolases - genetics
/ Amidohydrolases - metabolism
/ bacterial cell division
/ bacterial cell envelope
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Bacteriology
/ Cell Cycle Proteins - genetics
/ Cell Cycle Proteins - metabolism
/ Cell Division
/ coiled coils
/ Conformation
/ Cytoplasm
/ E coli
/ Enzyme Activation
/ Escherichia coli - enzymology
/ Escherichia coli - genetics
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - genetics
/ Escherichia coli Proteins - metabolism
/ Gene deletion
/ Molecular modelling
/ Mutagenesis, Site-Directed
/ Mutation
/ N-Acetylmuramoyl-L-alanine Amidase - genetics
/ N-Acetylmuramoyl-L-alanine Amidase - metabolism
/ Peptidoglycan - metabolism
/ peptidoglycan amidase
/ Peptidoglycans
/ Periplasmic space
/ Proteins
/ Research Article
/ Site-directed mutagenesis
/ structural microbiology
/ type VII ABC transporters
2025
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Probing the mechanism of peptidoglycan amidase activation by FtsEX-EnvC
by
Cook, Jonathan
, Crow, Allister
in
ABC transporter
/ ABC transporters
/ Amidase
/ Amidohydrolases - genetics
/ Amidohydrolases - metabolism
/ bacterial cell division
/ bacterial cell envelope
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Bacteriology
/ Cell Cycle Proteins - genetics
/ Cell Cycle Proteins - metabolism
/ Cell Division
/ coiled coils
/ Conformation
/ Cytoplasm
/ E coli
/ Enzyme Activation
/ Escherichia coli - enzymology
/ Escherichia coli - genetics
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - genetics
/ Escherichia coli Proteins - metabolism
/ Gene deletion
/ Molecular modelling
/ Mutagenesis, Site-Directed
/ Mutation
/ N-Acetylmuramoyl-L-alanine Amidase - genetics
/ N-Acetylmuramoyl-L-alanine Amidase - metabolism
/ Peptidoglycan - metabolism
/ peptidoglycan amidase
/ Peptidoglycans
/ Periplasmic space
/ Proteins
/ Research Article
/ Site-directed mutagenesis
/ structural microbiology
/ type VII ABC transporters
2025
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Probing the mechanism of peptidoglycan amidase activation by FtsEX-EnvC
by
Cook, Jonathan
, Crow, Allister
in
ABC transporter
/ ABC transporters
/ Amidase
/ Amidohydrolases - genetics
/ Amidohydrolases - metabolism
/ bacterial cell division
/ bacterial cell envelope
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Bacteriology
/ Cell Cycle Proteins - genetics
/ Cell Cycle Proteins - metabolism
/ Cell Division
/ coiled coils
/ Conformation
/ Cytoplasm
/ E coli
/ Enzyme Activation
/ Escherichia coli - enzymology
/ Escherichia coli - genetics
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - genetics
/ Escherichia coli Proteins - metabolism
/ Gene deletion
/ Molecular modelling
/ Mutagenesis, Site-Directed
/ Mutation
/ N-Acetylmuramoyl-L-alanine Amidase - genetics
/ N-Acetylmuramoyl-L-alanine Amidase - metabolism
/ Peptidoglycan - metabolism
/ peptidoglycan amidase
/ Peptidoglycans
/ Periplasmic space
/ Proteins
/ Research Article
/ Site-directed mutagenesis
/ structural microbiology
/ type VII ABC transporters
2025
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Probing the mechanism of peptidoglycan amidase activation by FtsEX-EnvC
Journal Article
Probing the mechanism of peptidoglycan amidase activation by FtsEX-EnvC
2025
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Overview
In E. coli , the FtsEX-EnvC system regulates two of the three division-associated amidases that break the peptidoglycan layer during bacterial division. Structural and mechanistic studies have revealed a detailed molecular mechanism for amidase activation in which an ABC transporter and its periplasmic partner reversibly activate periplasmic amidases under direction of the cytoplasmic cell division machinery. This paper explores structural features of EnvC that underpin autoinhibition and the activation mechanism. The FtsEX-EnvC system serves as a powerful example of a Type VII ABC transporter that uses transmembrane conformational changes to drive work in the periplasmic space.
Publisher
American Society for Microbiology,American Society for Microbiology (ASM)
Subject
/ Amidase
/ Amidohydrolases - metabolism
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Cell Cycle Proteins - genetics
/ Cell Cycle Proteins - metabolism
/ E coli
/ Escherichia coli - enzymology
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - genetics
/ Escherichia coli Proteins - metabolism
/ Mutation
/ N-Acetylmuramoyl-L-alanine Amidase - genetics
/ N-Acetylmuramoyl-L-alanine Amidase - metabolism
/ Proteins
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