Sandbox Reserved 1053: Difference between revisions
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== Biological Function == | == Biological Function == | ||
Czr A is a transcriptional repressor protein responsible for the regulation of the Chromosome Determined Zinc Responsible (Czr) operon. The Czr operon contains genes for the proteins Czr A and Czr B. Czr B is a Zinc transport protein which moves | Czr A is a transcriptional repressor protein responsible for the regulation of the Chromosome Determined Zinc Responsible (Czr) operon. The Czr operon contains genes for the proteins Czr A and Czr B. Czr B is a Zinc transport protein which moves Zn 2+ out of a cell. Czr A regulates this process by controlling the degree to which Czr B is expressed. When relatively low amounts of zinc are present in the cell Czr A will bind to DNA,preventing the progression of RNA polymerase and thus inhibiting expression of Czr B. Decreased expression of Czr B results in the ability of the cell to retain Zn 2+ more readily. Because Czr A and Czr B are transcribed as part of the same operon, there must be a way that Czr A is inhibited to allow full transcription of Czr B. Czr A is inhibited by the binding of two Zn 2+ ions, which is ideal considering that this mechanism allows for Zn 2+ concentration inside the cell to determine the need for Zn 2+ transport out of the cell. Zn 2+ competitively inhibits the binding of DNA to Czr A. Czr A has two distinct conformations, one of which binds Zn 2+ with very high affinity that has virtually no affinity towards DNA binding, the other having a high affinity for DNA binding but very little affinity for Zn 2+. | ||
===DNA Binding === | ===DNA Binding === | ||
===Zinc Binding === | ===Zinc Binding === | ||
Revision as of 13:31, 14 March 2017

| This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080. |
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Czr A Staphylococcus aureus
<StructureSection load='2kjc' size='340' side='right' caption='Caption for this structure' scene=>
This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Biological Function
Czr A is a transcriptional repressor protein responsible for the regulation of the Chromosome Determined Zinc Responsible (Czr) operon. The Czr operon contains genes for the proteins Czr A and Czr B. Czr B is a Zinc transport protein which moves Zn 2+ out of a cell. Czr A regulates this process by controlling the degree to which Czr B is expressed. When relatively low amounts of zinc are present in the cell Czr A will bind to DNA,preventing the progression of RNA polymerase and thus inhibiting expression of Czr B. Decreased expression of Czr B results in the ability of the cell to retain Zn 2+ more readily. Because Czr A and Czr B are transcribed as part of the same operon, there must be a way that Czr A is inhibited to allow full transcription of Czr B. Czr A is inhibited by the binding of two Zn 2+ ions, which is ideal considering that this mechanism allows for Zn 2+ concentration inside the cell to determine the need for Zn 2+ transport out of the cell. Zn 2+ competitively inhibits the binding of DNA to Czr A. Czr A has two distinct conformations, one of which binds Zn 2+ with very high affinity that has virtually no affinity towards DNA binding, the other having a high affinity for DNA binding but very little affinity for Zn 2+.
DNA Binding
Zinc Binding
Residues involved in Zn 2+ binding
Zinc Ligand(s)
This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
References
- ↑ 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:https://dx.doi.org/10.1002/ijch.201300024
- ↑ 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