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CTX-M Beta-Lactamase is an enzyme made to inhibit Beta-Lactam. It is found within bacteria, specifically the E. coli bacteria. Beta- Lactam binds with and cefotaxime, both of which are types of drugs made to fight bacterial infections. Beta-Lactam specifically attacks the lactam ring within both of these structures using a deacylation.

Biological relevance and broader implications

This enzyme inhibits the drug's function by breaking apart the lactam ring. This is does cause drug resistance within the E. coli bacteria making it much harder to treat.

Important amino acids

The important amino acids within the CTX-M Beta Lactamase are Ser70, Ser130, Lys234, Arg234, and Lys73. The residue at 234 does undergo a mutation in some cases and therefore can be either a Lys, or an Arg. The catalytic triad are the residues at 70, 130, and 234. The S130 helps to cleave the amide bond and distributes a proton to the nitrogen. S70 attacks the carbonyl carbon on the lactam ring before also protonating to create an alcohol and it breaks off again. K73 does work as a proton shuttle for both parts of the reaction.

Structural highlights

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

Other important features

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.