Results 11 to 20 of about 5,898 (109)

The role of the jaw subdomain of peptidoglycan glycosyltransferases for lipid II polymerization [PDF]

open access: yesThe Cell Surface, 2018
Bacterial peptidoglycan glycosyltransferases (PGT) catalyse the essential polymerization of lipid II into linear glycan chains required for peptidoglycan biosynthesis. The PGT domain is composed of a large head subdomain and a smaller jaw subdomain and can be potently inhibited by the antibiotic moenomycin A (MoeA). We present an X-ray structure of the
Punekar, Avinash S   +6 more
openaire   +5 more sources

SEDS glycosyltransferases in <i>E. faecalis</i> are upregulated by the CroS/R two-component system to enhance peptidoglycan synthesis during cell wall stress. [PDF]

open access: yesmSphere
ABSTRACT Enterococci are commensals of the intestinal tract that are intrinsically resistant to cephalosporins, antibiotics that inhibit peptidoglycan synthesis. Prior treatment with cephalosporins is a risk factor for acquiring an enterococcal infection.
Nelson ME   +3 more
europepmc   +3 more sources

The Role of the Substrate Lipid in Processive Glycan Polymerization by the Peptidoglycan Glycosyltransferases [PDF]

open access: yesJournal of the American Chemical Society, 2009
The peptidoglycan glycosyltransferases (PGTs) catalyze the processive polymerization of a C55 lipid-linked disaccharide (Lipid II) to form peptidoglycan, the main component of the bacterial cell wall. Our ability to understand this reaction has been limited due to challenges identifying the appropriate substrate analogues to selectively interrogate the
Deborah L, Perlstein   +4 more
openaire   +2 more sources

Structural Analysis of the Contacts Anchoring Moenomycin to Peptidoglycan Glycosyltransferases and Implications for Antibiotic Design [PDF]

open access: yesACS Chemical Biology, 2008
Peptidoglycan glycosyltransferases (PGTs), enzymes that catalyze the formation of the glycan chains of the bacterial cell wall, have tremendous potential as antibiotic targets. The moenomycins, a potent family of natural product antibiotics, are the only known active site inhibitors of the PGTs and serve as blueprints for the structure-based design of ...
Yanqiu Yuan   +5 more
openaire   +2 more sources

RodA as the missing glycosyltransferase in Bacillus subtilis and antibiotic discovery for the peptidoglycan polymerase pathway [PDF]

open access: yesNature Microbiology, 2017
The bacterial cell wall is a highly conserved essential component of most bacterial groups. It is the target for our most frequently used antibiotics and provides important small molecules that trigger powerful innate immune responses. The wall is composed of glycan strands crosslinked by short peptides.
Emami K   +7 more
openaire   +3 more sources

Isolated Peptidoglycan Glycosyltransferases from Different Organisms Produce Different Glycan Chain Lengths [PDF]

open access: yesJournal of the American Chemical Society, 2008
Peptidoglycan is an essential component of bacterial cell wall. The glycan strands of peptidoglycan are synthesized by enzymes called peptidoglycan glycosyltransferases (PGTs). Using a high-resolution SDS-PAGE assay, we compared the glycan strand lengths of four different PGTs from three different organisms (Escherichia coli, Enterococcus faecalis, and
Tsung-Shing Andrew, Wang   +3 more
openaire   +2 more sources

Bioinformatic approach of propolis as an inhibitor of peptidoglycan glycosyltransferase to improve antibacterial agent: An in-silico study

open access: yesDental Journal, 2021
Background: In Indonesia, the prevalence of dental and oral problems is still high at 57.6% in 2018, especially periodontitis at 74.1%. Peptidoglycan is an essential component of the bacterial cell wall. Peptidoglycan glycosyltransferase (PGT) is a protein target that plays a role in transferring lipid disaccharides II to growing glycan chains for ...
Sani, Imelia Arifatus   +4 more
openaire   +4 more sources

Correction: Corrigendum: RodA as the missing glycosyltransferase in Bacillus subtilis and antibiotic discovery for the peptidoglycan polymerase pathway [PDF]

open access: yesNature Microbiology, 2017
Nature Microbiology 2, 16253 (2017); published online 13 January 2017; corrected 30 January 2017 The original version of this Article was published without Supplementary Tables 1 and 2. This has now been corrected so that both tables are available online.
Kaveh, Emami   +7 more
openaire   +2 more sources

The MurG glycosyltransferase provides an oligomeric scaffold for the cytoplasmic steps of peptidoglycan biosynthesis in the human pathogen Bordetella pertussis [PDF]

open access: yesScientific Reports, 2019
AbstractPeptidoglycan is a major component of the bacterial cell wall and thus a major determinant of cell shape. Its biosynthesis is initiated by several sequential reactions catalyzed by cytoplasmic Mur enzymes. Mur ligases (MurC, -D, -E, and -F) are essential for bacteria, metabolize molecules not present in eukaryotes, and are structurally and ...
Laddomada, Federica   +10 more
openaire   +4 more sources

The monofunctional glycosyltransferase of Escherichia coli is a member of a new class of peptidoglycan‐synthesising enzymes [PDF]

open access: yesFEBS Letters, 1996
Using conserved fingerprints in the glycosyltransferase (GTase) domain of high‐molecular‐weight penicillin‐binding proteins (PBP), a gene (mgt) encoding a putative monofunctional glycosyltransferase has been identified in Haemophilus influenzae and in other bacterial species.
Di Berardino, Marco   +4 more
openaire   +1 more source

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