User:Holly Rowe/Sandbox 1

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=''Mitochondrial Calcium Uniporter''=
=''Mitochondrial Calcium Uniporter''=
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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<StructureSection load='6DT0' size='350' frame='true' side='right' caption='Mitochondrial Calcium Uniporter 6DT0' scene=’’>
This is a default text for your page '''Holly Rowe/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
This is a default text for your page '''Holly Rowe/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
==Introduction==
==Introduction==
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===Structure===
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[https://www.rcsb.org/structure/6dt0 Calcium Uniporter PDB File]
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Calcium is a very important signaling molecule in the body with many physiological functions including muscle contraction, neuron excitability, cell migration and growth. The mitochondria are important regulators of calcium in the body and the calcium uniporter (MCU) maintains calcium homeostasis within the mitochondria. Calcium moves in one direction from the intermembrane space through the inner mitochondrial membrane into the matrix. The matrix is more negative driven by the respiratory chain which draws calcium in and allows calcium to move down its gradient.
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The MCU is a complex. Its MICU1 and MICU2 bind together and associate with EMRE which regulates MCU. The MICU1 and MICU2 act as gatekeepers. EMRE connects the MICU1 and MICU2 sensors to MCU therefore regulating calcium uptake for the protein
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<scene name='83/837219/Selectivity_pore/1'>Selectivity Pore</scene>
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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.]]
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[https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy] Cryogenic electron microscopy (Cryo-EM) was instrumental in outlining the complete structure of this protein.
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==Structure==
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[[Image:Bubble_pic.png|300 px|right|thumb|Figure 2 Representation of the calcium fitting into the selectivity pore.]]
== Function ==
== Function ==
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== References ==
== References ==
<references/>
<references/>
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<ref name=”Ransey”>PMID:28504306</ref>
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==Student Contributors==
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*Holly Rowe
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*Lizzy Ratz
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*Maddi Summers

Current revision

Mitochondrial Calcium Uniporter

Mitochondrial Calcium Uniporter 6DT0

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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

[1]

Student Contributors

  • Holly Rowe
  • Lizzy Ratz
  • Maddi Summers

Proteopedia Page Contributors and Editors (what is this?)

Holly Rowe

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