Sandbox Wabash 06 Fumarase

From Proteopedia

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== True Active Site ==
== True Active Site ==
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In lieu of the fact that a histidine side chain was one of the bases in the catalytic reaction, in order to determine which of the two sites was indeed the active site, histidines could be observed. By mutating the histidines at the two active sites, one would be able to determine that if the A-site was active, changing the H188 chain would dramatically affect the catalytic activity. Rather, if the B-site was the active site, then a mutation in H129 would affect catalysis.
== Structural highlights ==
== Structural highlights ==
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A histidine at each of the sites was mutated to an asparagine. The H188N mutation at the A-site resulted in a large decrease in specific activity. Rather, the H129N mutation at the B-site resulted in no change in activity.
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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.
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.

Revision as of 22:26, 28 February 2016

Mutations in Fumerase Active Site

Caption for this structure

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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
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