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Function

^[1] is a serine protease that is found in the bacteria Vibrio cholerae. The function of VesB is to contribute to intestinal growth and pathogenesis. VesB is also able to cleave peptide bonds in proteins after arginines. This means that the substrate of VesB would be a protein containing arginine, or multiple arginines (XXRXX) and the product after cleavage is all of the protein through the arginine, and the rest of the protein(XXR + XX), or the rest of the protein through the next arginine, if there are multiple.

Disease

VesB has been detected in vibrio cholerae from patients with clinical cholera. VesB is able to cleave the A subunit of cholera toxin, which is a process that leads to the activation of cholera toxin. Cholera toxin is then released into the intestine, causing Cholera. When the toxin is released, it causes rapid fluid loss and severe dehydration.

Relevance

Structural highlights

VesB's is made up mostly of beta sheets with some alpha helices and random coil. VesB has that make up it's tertiary/quaternary structure. It has a N-terminal protease domain with a trypsin/chymotrypsin-fold and a C-terminal Ig-fold domain.

This crystal structure was solved without a ligand, but the VesB ligand is known to be any protein containing Arg-X.

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.