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Structure and Mechanism of the Glycerol-3-Phosphate Transporter from Escherichia coli
TLDR
This work reports the 3.3 angstrom resolution structure of a member of the major facilitator superfamily, GlpT, which transports glycerol-3-phosphate into the cytoplasm and inorganic phosphate into the periplasm and proposes that it operates by a single–binding site, alternating-access mechanism through a rocker-switch type of movement. Expand
Crystallographic structure of human beta-hexosaminidase A: interpretation of Tay-Sachs mutations and loss of GM2 ganglioside hydrolysis.
TLDR
NGT, a mechanism-based inhibitor, has been shown to act as a chemical chaperone that prevents misfolding of a Hex A mutant associated with adult onset Tay Sachs disease and, as a result, increases the residual activity of Hex A to a level above the critical threshold for disease. Expand
The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis
TLDR
The structural results on these rhomboid peptidases have allowed us to speculate on the catalytic mechanism of substrate cleavage in a membranous environment and to identify the relative disposition of the nucleophilic serine to the general base/acid function of the conserved histidine. Expand
Practical aspects of overexpressing bacterial secondary membrane transporters for structural studies.
TLDR
In this review, those factors that affect the quantity and quality of the protein produced are analyzed, and recent progress in overexpression of membrane transporters from bacterial inner membrane is summarized. Expand
The structural basis of substrate translocation by the Escherichia coli glycerol-3-phosphate transporter: a member of the major facilitator superfamily.
TLDR
The crystal structure suggests that the glycerol-3-phosphate transporter operates through a single binding site, alternating access mechanism via a rocker-switch type of movement of the N- and C-terminal domains. Expand
Feline coronavirus drug inhibits the main protease of SARS-CoV-2 and blocks virus replication
TLDR
GC373 and GC376 are potent inhibitors of SARS-CoV-2 in cell culture, with EC50 values near one micromolar and little to no toxicity and the framework for their use in human trials for the treatment of COVID-19 is laid. Expand
Allosteric regulation of rhomboid intramembrane proteolysis
TLDR
It is revealed that exosite formation is dependent on the oligomeric state of rhomboids, and when dimers are dissociated, allosteric substrate activation is not observed, indicating allostery plays a role in substrate catalysis. Expand
Three‐dimensional crystallization of the Escherichia coli glycerol‐3‐phosphate transporter: A member of the major facilitator superfamily
TLDR
The successful three‐dimensional crystallization of GlpT, the glycerol‐3‐phosphate transporter from Escherichia coli inner membrane, is reported, with better‐ordered crystals than previously reported. Expand
Glycerol-3-phosphate transporter of Escherichia coli: structure, function and regulation.
TLDR
The crystal structure of GlpT suggests a single binding site, alternating access mechanism for substrate translocation, namely, the substrate bound at the N- and C-terminal domain interface is transported across the membrane via a rocker-switch type of movement of the domains. Expand
Domain swapping in the cytoplasmic domain of the Escherichia coli rhomboid protease.
TLDR
An extensive steady-state kinetic analysis of the full-length ecGlpG and its membrane domain using soluble and transmembrane model protein substrates resulted in an unexpected conclusion: removal of the cytoplasmic domain does not alter the catalytic parameters for detergent-solubilized rhomboid for both substrates. Expand
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