Sandbox Reserved 994

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This Sandbox is Reserved from 20/01/2015, through 30/04/2016 for use in the course "CHM 463" taught by Mary Karpen at the Grand Valley State University. This reservation includes Sandbox Reserved 987 through Sandbox Reserved 996.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

OXA-24 β-lactamase

Caption for this structure

Drag the structure with the mouse to rotate

References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
  3. ↑ PMID:162717<ref>. β-lactams mimic the structure of the usual PBP substrate and therefore disrupt the cross-linking process that is critical to cell wall synthesis. Once the β-lactam ring binds, the PBP is irreversibly inactivated. As a result, the bacterial cell wall is compromised, and the bacteria lyse and die (Patrick, 2005). Due to overperscription and misuse of antibiotics, bacteria have been able to develop resistance mechanisms. One of these resistance mechanisms is through the expression of β-lactamases. β-lactamases act by cleaving the -lactam ring and render the antibiotic inactive before it has a chance to inhibit the transpeptidase enzymes (Neu, 1992). β-lactamases are grouped into four different classes: A, B, C and D, all of which (besides class B) use a serine based mechanism for destruction of β-lactams. Class B β-lactamases use zinc ions for hydrolysis. In 1980, R.P. Ambler described the first two classes of β-lactamases: Class A and B. Class A were expressed by S. aureus and class B were expressed by B. cereus. Afterwards, Jaurin and Grundstorm observed class C enzymes which hydrolyzes cephalosporins. Class D was distinguished from other serine β-lactamase in the late 1980s, due to having an affinity to oxacillin as its substrate in addition to carbapenems (2). Even more concerning is that the class D β-lactamases, or OXAs, are not inhibited by current clinical β-lactamase inhibitors, such as clavulanic acid. OXA-24 poses a high clinical threat due to its lack of an effective inhibitor. == CHDLs == == Structure == == Hydrolysis Mechanism == [[Image:B-lactam hydrolysis.png]] == Inhibition == This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. </li></ol></ref>
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