User:Holly Rowe/Sandbox 1: Difference between revisions
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<scene name='83/837219/Selectivity_pore/1'>Selectivity Pore</scene> | <scene name='83/837219/Selectivity_pore/1'>Selectivity Pore</scene> | ||
The selectivity pore is an integral part of the protein. This pore contains a group of glutamate with oxygen facing inward forming a carboxylate ring through which calcium enters. This negative carboxylate ring does a good job of pulling the positive calcium into the selectivity pore at the top of the protein. [[Image:carboxylate_ring.png|300 px|right|thumb|Figure 1 Carboxylate ring within the selectivity pore.]] | The selectivity pore is an integral part of the protein. This pore contains a group of glutamate with oxygen facing inward forming a carboxylate ring through which calcium enters. This negative carboxylate ring does a good job of pulling the positive calcium into the selectivity pore at the top of the protein. [[Image:carboxylate_ring.png|300 px|right|thumb|Figure 1 Carboxylate ring within the selectivity pore.]] | ||
[https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy] Cryogenic electron microscopy (Cryo-EM) was instrumental in outlining the complete structure of this protein. | |||
==Structure== | ==Structure== | ||
Latest revision as of 01:03, 6 April 2020
Mitochondrial Calcium Uniporter
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References
Student Contributors
- Holly Rowe
- Lizzy Ratz
- Maddi Summers
- ↑ Ransey E, Paredes E, Dey SK, Das SR, Heroux A, Macbeth MR. Crystal structure of the Entamoeba histolytica RNA lariat debranching enzyme EhDbr1 reveals a catalytic Zn(2+) /Mn(2+) heterobinucleation. FEBS Lett. 2017 Jul;591(13):2003-2010. doi: 10.1002/1873-3468.12677. Epub 2017, Jun 14. PMID:28504306 doi:https://dx.doi.org/10.1002/1873-3468.12677

