RNA Polymerase II
From Proteopedia
(Difference between revisions)
| Line 5: | Line 5: | ||
== Overview == | == Overview == | ||
| + | RNA polymerase (RNAP) II | ||
| - | == Components == | + | == Structural Components == |
The clamp swings to trap the DNA in the cleft. Further along, the wall sends the DNA template through the cleft in approximately a 90° turn. Both the clamp and wall are parts of the Rpb2 subunit. Further along in the process, the rudder separates the newly synthesized RNA strand from the DNA template. The DNA reforms into a double helix as it leaves RNA pol II. | The clamp swings to trap the DNA in the cleft. Further along, the wall sends the DNA template through the cleft in approximately a 90° turn. Both the clamp and wall are parts of the Rpb2 subunit. Further along in the process, the rudder separates the newly synthesized RNA strand from the DNA template. The DNA reforms into a double helix as it leaves RNA pol II. | ||
| Line 12: | Line 13: | ||
The jaw is the opening through which DNA enters. The funnel is what the NTP’s travel through to be incorporated into the growing RNA strand, and the pore is the end of the funnel. The bridge is an Rpb1 segment that translocates the DNA-RNA combination at the end of each cycle of catalysis. | The jaw is the opening through which DNA enters. The funnel is what the NTP’s travel through to be incorporated into the growing RNA strand, and the pore is the end of the funnel. The bridge is an Rpb1 segment that translocates the DNA-RNA combination at the end of each cycle of catalysis. | ||
| + | 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. | ||
| - | == | + | == Mechanism of Action == |
| - | == | + | == Alpha Amanitin == |
| + | α-Amanitin is a bicyclinc octapeptide that adheres tightly with RNAP II, which blocks the elongation steps. α-amanitin binds in the funnel and interacts with the bridge helix and adjacent Rpb1, but it does not inhibit the RNA pol II’s interaction with NTP. Instead, α-amanitin likely challenges the bridge’s conformational change that is necessary for the purposed RNAP translocation step. α-Amanitin, found in the poisonous mushroom death cap, leads to death after several days. This time frame aligns with the rate at which mRNA’s and proteins turnover. | ||
| + | |||
| + | == Modifications == | ||
| - | == Relevance == | ||
| - | == Structural highlights == | ||
| - | 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. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 23:22, 30 September 2019
Your Heading Here (maybe something like 'Structure')
| |||||||||||
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:http://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
Proteopedia Page Contributors and Editors (what is this?)
Titus Edwards, Abraham Kiesel, Wally Novak, James Daniel Andry, Michal Harel, Karsten Theis
