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Mutational Replacements at the "glycine Hinge" of the Escherichia coli Chemoreceptor Tsr Support a Signaling Role for the C-Helix Residue
(American Chemical Society, 2017-07)
Bacterial chemoreceptors are dimeric membrane proteins that transmit signals from a periplasmic ligand-binding domain to the interior of the cells. The highly conserved cytoplasmic domain consists of a long hairpin that ...
Mutational Replacements at the “Glycine Hinge” of the Escherichia coli Chemoreceptor Tsr Support a Signaling Role for the C-Helix Residue
(American Chemical Society, 2017-06)
Bacterial chemoreceptors are dimeric membrane proteins that transmit signals from a periplasmic ligand-binding domain to the interior of the cells. The highly conserved cytoplasmic domain consists of a long hairpin that ...
Obtaining an Ent35-MccV derivative with mutated hinge region that exhibits increased activity against listeria monocytogenes and escherichia coli
(Springer, 2019-11)
The present paper describes the generation of derivatives from the hybrid peptide called Ent35-MccV, active against Gram-positive and Gram-negative bacteria. This peptide has a triple glycine hinge region between enterocin ...
IDENTIFICATION OF A PUTATIVE MEMBRANE-INSERTED SEGMENT IN THE ALPHA-TOXIN OF STAPHYLOCOCCUS-AUREUS
(Amer Chemical Soc, 1994-06-14)
To gain a fuller understanding of the regions of the Staphylococcus aureus alpha-toxin important in pore formation, we have used Forster dipole-dipole energy transfer to demonstrate that a central glycine-rich region of ...
IDENTIFICATION OF A PUTATIVE MEMBRANE-INSERTED SEGMENT IN THE ALPHA-TOXIN OF STAPHYLOCOCCUS-AUREUS
(Amer Chemical Soc, 1994-06-14)
To gain a fuller understanding of the regions of the Staphylococcus aureus alpha-toxin important in pore formation, we have used Forster dipole-dipole energy transfer to demonstrate that a central glycine-rich region of ...
IDENTIFICATION OF A PUTATIVE MEMBRANE-INSERTED SEGMENT IN THE ALPHA-TOXIN OF STAPHYLOCOCCUS-AUREUS
(Amer Chemical Soc, 2014)
The inhibition of 5-enolpyruvylshikimate-3-phosphate synthase as a model for development of novel antimicrobials
(2007-03-01)
EPSP synthase (EPSPS) is an essential enzyme in the shikimate pathway, transferring the enolpyruvyl group of phosphoenolpyruvate to shikimate-3-phosphate to form 5-enolpyruvyl-3-shikimate phosphate and inorganic phosphate. ...
The inhibition of 5-enolpyruvylshikimate-3-phosphate synthase as a model for development of novel antimicrobials
(2007-03-01)
EPSP synthase (EPSPS) is an essential enzyme in the shikimate pathway, transferring the enolpyruvyl group of phosphoenolpyruvate to shikimate-3-phosphate to form 5-enolpyruvyl-3-shikimate phosphate and inorganic phosphate. ...