Sandbox Reserved 1674
From Proteopedia
(Difference between revisions)
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==CTX-M Beta-Lactamase== | ==CTX-M Beta-Lactamase== | ||
<StructureSection load='7K2X' size='340' side='right' caption='Overall structure of CTX-M Beta-Lactamase without any important ligands. (PDB: 7K2X)' 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 the E.Coli bacteria and makes the bacteria drug resistant. | |
- | + | ||
== Structure == | == Structure == | ||
- | 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 catalytic amino acids, which have been highlighted here. | + | 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 catalytic amino acids, which have been highlighted <scene name='87/873236/Active_site_red/1'>here</scene>. |
== Disease == | == Disease == | ||
Revision as of 00:57, 29 March 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
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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