Sandbox Reserved 1674: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
{{Sandbox_Reserved_BHall_Sp21}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_BHall_Sp21}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
==CTX-M Beta-Lactamase== | ==CTX-M Beta-Lactamase== | ||
== Function of your protein == | == Function of your protein == | ||
Beta- Lactam binds with<scene name='87/873236/Ampicillin/1'> ampicillin</scene> | <StructureSection load='7K2X' size='340' side='right' caption='Overall structure of CTX-M Beta-Lactamase without any important ligands. (PDB: 7K2X)' scene=''> | ||
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<scene name='87/873236/Ampicillin/1'> ampicillin</scene> 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 == | == 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== | == 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 == | == Structural highlights == | ||
This protein has eight chains. <scene name='87/873236/Chain_a/1'>Each chain</scene> 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<scene name='87/873236/Chain_a_active_site/1'>e catalytic amino acids</scene>, which have been highlighted <scene name='87/873236/Active_site_red/1'>here</scene>. | This protein has eight chains. <scene name='87/873236/Chain_a/1'>Each chain</scene> 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<scene name='87/873236/Chain_a_active_site/1'>e catalytic amino acids</scene>, which have been highlighted <scene name='87/873236/Active_site_red/1'>here</scene>. | ||
