Results 51 to 60 of about 20,249 (205)

Binding site‐shaped repeated sequences of bacterial wall peptidoglycan hydrolases [PDF]

open access: yesFEBS Letters, 1994
The non‐catalytic C‐terminal regions of the N‐acetylmuramidase (lysozyme) of Clostridium acetobutylicum and N‐acetylmuramoyl(d‐lactyl)‐l‐alanine amidases CwlA of Bacillus subtilis, ORFL3 and CwlL of Bacillus licheniformis were previously reported to have similarities with the amino acid sequence of the non‐catalytic N‐terminal module of the ...
Ghuysen, Jean-Marie   +3 more
openaire   +2 more sources

Comparative Phylogenomics of Pathogenic and Nonpathogenic Species. [PDF]

open access: yes, 2015
The Ascomycete Onygenales order embraces a diverse group of mammalian pathogens, including the yeast-forming dimorphic fungal pathogens Histoplasma capsulatum, Paracoccidioides spp. and Blastomyces dermatitidis, the dermatophytes Microsporum spp.
Taylor, John W, Whiston, Emily
core   +3 more sources

DipM, a new factor required for peptidoglycan remodelling during cell division in Caulobacter crescentus [PDF]

open access: yes, 2010
In bacteria, cytokinesis is dependent on lytic enzymes that facilitate remodelling of the cell wall during constriction. In this work, we identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in ...
Aaron   +88 more
core   +3 more sources

Carbohydrate recognition and lysis by bacterial peptidoglycan hydrolases

open access: yesCurrent Opinion in Structural Biology, 2017
The major component of bacterial cell wall is peptidoglycan (PG), a complex polymer formed by long glycan chains cross-linked by peptide stems. PG is in constant equilibrium requiring well-orchestrated coordination between synthesis and degradation. The resulting cell-wall fragments can be recycled, act as messengers for bacterial communication, as ...
Alcorlo, Martín   +3 more
openaire   +3 more sources

Toxin release mediated by the novel autolysin Cwp19 in Clostridium difficile

open access: yesMicrobial Cell, 2018
Clostridium difficile, also known as Clostriodioides difficile, is a Gram positive, spore-forming bacterium and a leading cause of antibiotic-associated diarrhea in nosocomial environments. The key virulence factors of this pathogen are two toxins, toxin
Imane El Meouche, Johann Peltier
doaj   +1 more source

Interaction of Mycobacterium tuberculosis Virulence Factor RipA with Chaperone MoxR1 Is Required for Transport through the TAT Secretion System

open access: yesmBio, 2016
Mycobacterium tuberculosis is a leading cause of death worldwide. The M. tuberculosis TAT (twin-arginine translocation) protein secretion system is present at the cytoplasmic membrane of mycobacteria and is known to transport folded proteins.
Manish Bhuwan   +7 more
doaj   +1 more source

A mycobacterial enzyme essential for cell division synergizes with resuscitation-promoting factor. [PDF]

open access: yesPLoS Pathogens, 2008
The final stage of bacterial cell division requires the activity of one or more enzymes capable of degrading the layers of peptidoglycan connecting two recently developed daughter cells. Although this is a key step in cell division and is required by all
Erik C Hett   +3 more
doaj   +1 more source

Coordinated peptidoglycan synthases and hydrolases stabilize the bacterial cell wall

open access: yesNature Communications, 2023
Abstract Peptidoglycan (PG) defines cell shape and protects bacteria against osmotic stress. The growth and integrity of PG require coordinated actions between synthases that insert new PG strands and hydrolases that generate openings to allow the insertion.
Huan Zhang   +3 more
openaire   +3 more sources

Structural basis of adaptor-mediated protein degradation by the tail-specific PDZ-protease Prc

open access: yesNature Communications, 2017
MepS is a peptidoglycan (PG) cross-link specific hydrolase needed for cell wall expansion and its cellular levels must be tightly regulated. Here the authors present the structure of the MepS degrading protease Prc bound to its adaptor NlpI and propose a
Ming-Yuan Su   +11 more
doaj   +1 more source

Structural Investigations on the SH3b Domains of Clostridium perfringens Autolysin through NMR Spectroscopy and Structure Simulation Enlighten the Cell Wall Binding Function

open access: yesMolecules, 2021
Clostridium perfringens autolysin (CpAcp) is a peptidoglycan hydrolase associated with cell separation, division, and growth. It consists of a signal peptide, ten SH3b domains, and a catalytic domain.
Yubao Shan   +6 more
doaj   +1 more source

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