Sandbox Reserved 1674
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The important amino acids within the CTX-M Beta Lactamase are Ser70, Ser130, Lys234, Arg234, and Lys73. This creates the <scene name='87/873236/Active_site/2'>catalytic triad</scene> with one proton shuttle. 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. | The important amino acids within the CTX-M Beta Lactamase are Ser70, Ser130, Lys234, Arg234, and Lys73. This creates the <scene name='87/873236/Active_site/2'>catalytic triad</scene> with one proton shuttle. 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 | + | 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 those<scene name='87/873236/Chain_a_active_site/1'> catalytic amino acids</scene>. |
| + | The important<scene name='87/873236/Amino_acid_tert/1'> tertiary structure</scene> is how the protein folds to allow the amino acids in the catalytic triad to be near each other because in the sequence, the amino acids are not near each other. By folding, the protein is able to create the binding pocket that holds the catalytic amino acids that help Beta- Lactamase function normally. | ||
== Other important features == | == Other important features == | ||
Revision as of 02:58, 19 April 2021
| This Sandbox is Reserved from 01/25/2021 through 04/30/2021 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1665 through Sandbox Reserved 1682. |
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CTX-M Beta-Lactamase
CTX-M Beta Lactamase is a class A enzyme that creates drug resistance to ampicillin and cefotaxime through. two step process of deacylation and acylation.
Function of your protein
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References
- ↑ Soeung V, Lu S, Hu L, Judge A, Sankaran B, Prasad BVV, Palzkill T. A drug-resistant beta-lactamase variant changes the conformation of its active-site proton shuttle to alter substrate specificity and inhibitor potency. J Biol Chem. 2020 Dec 25;295(52):18239-18255. doi: 10.1074/jbc.RA120.016103. Epub, 2020 Oct 26. PMID:33109613 doi:http://dx.doi.org/10.1074/jbc.RA120.016103
