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Oxybenzone or benzophenone-3 or BP-3 (trade names Milestab 9, Eusolex 4360, Escalol 567, KAHSCREEN BZ-3) is an organic compound belonging to the class of aromatic ketones known as benzophenones. It takes the form of pale-yellow crystals that are readily soluble in most organic solvents.
Proteins of the Proton-dependent Oligopeptide Transporter (POT) Family (also called the PTR (peptide transport) family) are found in animals, plants, yeast, archaea and both Gram-negative and Gram-positive bacteria, and are part of the major facilitator superfamily. The transport of peptides into cells is a well-documented biological phenomenon ...
Bacterial Leucine Transporter (LeuT) is a bundled twelve alpha helix protein which belongs to the family of transporters that shuttle amino acids in and out of bacterial cells. Specialized in small hydrophobic amino acids such as leucine and alanine , this transporter is powered by the gradient of sodium ions that is normally maintained by ...
The general secretion (Sec) involves secretion of unfolded proteins that first remain inside the cells. In Gram-negative bacteria, the secreted protein is sent to either the inner membrane or the periplasm. But in Gram-positive bacteria, the protein can stay in the cell or is mostly transported out of the bacteria using other secretion systems.
The integral inner-membrane proteins translocate the substrate across the membrane. It has been shown, [3] [4] that most of these proteins contain a conserved region located about 80 to 100 residues from their C-terminal extremity. This region seems [5] to be located in a cytoplasmic loop between two transmembrane domains.
These proteins are typically virulence factors, associated with infection or virulence in pathogenic bacteria. The name autotransporter derives from an initial understanding that the protein was self-sufficient in transporting the passenger domain through the outermembrane. This view has since been challenged by Benz and Schmidt. [2]
These proteins are predicted to have 12 alpha-helical transmembrane regions, some of the animal proteins may have an additional C-terminal helix. [4] The X-ray structure of the NorM was determined to 3.65 Å, revealing an outward-facing conformation with two portals open to the outer leaflet of the membrane and a unique topology of the predicted 12 transmembrane helices distinct from any other ...
The first structure of a bacterial microcompartment shell, determined by X-ray crystallography and cryo-electron microscopy [1] contains representatives of each of the shell protein types: BMC-P, BMC-H and BMC-T, in both its trimer (upper right) and dimer of trimer (lower right), forms.