Sandbox 1666

This is a default text for your page Sandbox 1666. Click above on edit this page to modify. Be careful with the < and > signs.

You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

Function of Protein

This protein is produced in bacteria, more specifically E. coli. CTX-M Beta-Lactamase is produced in bacteria which causes drug resistance in B-lactam antibiotics, also known as penicillin. It attacks the amide bond in the lactam anitbiotics, which causes deacylation to occur. is the overall structure of CTX-M Beta-Lactamase.

Biological Relevance and Broader Implications

This protein causes drug resistance, which is a problem. It is a problem because if we can understand it better, we can change the way we treat it to fight off the bacteria better.

Important Amino Acids

An important ligand of this protein is GOL (glycerol), which is the only ligand in this protein. GOL helps with stability of this protein. The catalytic amino acids of this protein include Ser^70, Ser^130, and Lys^73. Ser^70 interacts with the oxygen on the ampicillin, and it is also cross-linked with clavulanic acid. Ser^130 is also cross-linked with clavulanic acid and interacts with the ligand through hydrogen bonds. Lys^73 also interacts with the ligand through hydrogen bonds. This amino acid is used to lower the pka value of the hydroxyl group as well.

Structural highlights

This protein has eight chains. Each chain has eleven separate alpha helices and nine separate beta sheets. Some of the chains bind to GOL to help with stability. Within each chain, there are two of the catalytic amino acid within helix three. The last catalytic amino acid is located in helix seven. Both of these helices form important interactions with the ligands because of those catalytic amino acids, which have been highlighted here.

Other Important Features