User:Jessica Klingensmith/Sandbox 1068
From Proteopedia
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| - | == | + | ==Zinc Transporter YiiP== 2 |
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
This is a default text for your page '''Jessica Klingensmith/Sandbox 1068'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page '''Jessica Klingensmith/Sandbox 1068'''. 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 <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. | ||
| - | == | + | == Importance of Zinc Transporters == |
| - | == | + | == Introduction to YiiP Structure == |
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| + | YiiP is an integral membrane protein found in the membrane of Esherichia coli. YiiP is composed of dimers with each monomer consisting of 238 residues. YiiP has a "Y" shape conformation with two different functional conformations. A total of six helices comprise the transmembrane portion of each monomer (GREEN). Four of these helices are bundled together while the remaining two are oriented antiparallel to the bundle (GREEN). Movement of these helices play a role in the function of YiiP. An interlocked salt bridge connects the two domains with the Lys77 and the Asp207 from each domain - visualized here: (GREEN).This salt bridge acts as the hinge for the conformational changes that YiiP undergoes.Hydrophobic residues (GREEN) beneath the salt bridge further stabilize the two domains in the v-shaped void where the domains connect. YiiP has three zinc binding sites, two of which are known to play an active role in the function of YiiP. Site A (link) sits in extracellular space outside of the cell, while site C is situated inside of the cell to act as a sensor of intracellular zinc concentrations. | ||
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| + | ==Function == | ||
| + | YiiP functions to export zinc out of the cytoplasm of cells in order to regulate zinc levels within the cell. It is a member of the cation diffusion facilitator family (LINK) and works via secondary transport and two conformations to sense zinc in the cell and transport zinc out of the cell into extracellular space using an electrochemical gradient of H+ ins antiported with zinc. The presence of cytoplasmic zinc (bound in the c-terminus domain) activates conformational changes that translocate the metal ions across the membrane and out of the cell. | ||
| - | == Relevance == | ||
== Structural highlights == | == Structural highlights == | ||
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| + | ===The Interlocking Salt Bridge=== | ||
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| + | ===Active Sites=== | ||
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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 17:51, 17 March 2017
==Zinc Transporter YiiP== 2
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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
