Results 41 to 50 of about 11,450 (169)

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

Prediction of peptidoglycan hydrolases- a new class of antibacterial proteins [PDF]

open access: yesBMC Genomics, 2016
The efficacy of antibiotics against bacterial infections is decreasing due to the development of resistance in bacteria, and thus, there is a need to search for potential alternatives to antibiotics. In this scenario, peptidoglycan hydrolases can be used as alternate antibacterial agents due to their unique property of cleaving peptidoglycan cell wall ...
Sharma, Ashok K.   +4 more
openaire   +2 more sources

More than just lysins: peptidoglycan hydrolases tailor the cell wall [PDF]

open access: yesCurrent Opinion in Microbiology, 2011
Enzymes that degrade the peptidoglycan (PG) cell wall layer called PG hydrolases or autolysins are often thought of as destructive forces. Phages employ them to lyse their host for the release of virion particles and some bacteria secrete them to eliminate (lyse) their competition.
Tsuyoshi, Uehara, Thomas G, Bernhardt
openaire   +2 more sources

The DigH glycosyl hydrolase is conditionally required for daughter cell separation in Escherichia coli

open access: yesJournal of Bacteriology
The peptidoglycan (PG) cell wall is a mesh-like layer that shapes bacteria and protects against osmotically induced lysis. PG is composed of glycan strands and peptide chains that link together to form a continuous layer that surrounds the cell.
Joseph C. Bryant   +5 more
doaj   +1 more source

Bacteria‐Responsive Nanostructured Drug Delivery Systems for Targeted Antimicrobial Therapy

open access: yesAdvanced Materials, EarlyView.
Bacteria‐responsive nanocarriers are designed to release antimicrobials only in the presence of infection‐specific cues. This selective activation ensures drug release precisely at the site of infection, avoiding premature or indiscriminate release, and enhancing efficacy.
Guillermo Landa   +3 more
wiley   +1 more source

Structural basis of the novel S. pneumoniae virulence factor, GHIP, a glycosyl hydrolase 25 participating in host-cell invasion. [PDF]

open access: yesPLoS ONE, 2013
Pathogenic bacteria produce a wide variety of virulence factors that are considered to be potential antibiotic targets. In this study, we report the crystal structure of a novel S.
Siqiang Niu   +15 more
doaj   +1 more source

Home - About - Disclaimer - Privacy