Sandbox Reserved 1069: Difference between revisions

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OCA, Geoffrey C. Hoops, Madison Walberry, Austin S. Moore, Jessica Klingensmith, Kyle Colston

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	YiiP is a homodimer, with each monomer consisting of 238 residues [https://en.wikipedia.org/wiki/Protein_dimer (protein dimer)] with a TransMembrane (<scene name='69/694236/Tmd/1'>TMD</scene>) and C-Terminal (<scene name='69/694236/Ctd/1'>CTD</scene>) domain that are connected via a charge interlocking mechanism located on a flexible loop. The TMD, where Zn<sup>2+</sup> binding site A resides, consists of a total of six helices in each <scene name='75/756372/Sixhelices/1'>monomer</scene>. Four of these helices are bundled together while the remaining two are oriented antiparallel to the <scene name='75/756372/2antiparallel/1'>bundle</scene>. Movement of these helices play a role in the function of YiiP. A large portion of the protein containing binding site C, the <scene name='69/694236/Ctd/1'>CTD</scene> , approximately 30 Å in length<sup>[https://www.bnl.gov/isd/documents/71335.pdf]</sup>, protrudes into the cytoplasm functioning as a zinc sensor within the cell.		YiiP is a homodimer, with each monomer consisting of 238 residues [https://en.wikipedia.org/wiki/Protein_dimer (protein dimer)] with a TransMembrane (<scene name='69/694236/Tmd/1'>TMD</scene>) and C-Terminal (<scene name='69/694236/Ctd/1'>CTD</scene>) domain that are connected via a charge interlocking mechanism located on a flexible loop. The TMD, where Zn<sup>2+</sup> binding site A resides, consists of a total of six helices in each <scene name='75/756372/Sixhelices/1'>monomer</scene>. Four of these helices are bundled together while the remaining two are oriented antiparallel to the <scene name='75/756372/2antiparallel/1'>bundle</scene>. Movement of these helices play a role in the function of YiiP. A large portion of the protein containing binding site C, the <scene name='69/694236/Ctd/1'>CTD</scene> , approximately 30 Å in length<sup>[https://www.bnl.gov/isd/documents/71335.pdf]</sup>, protrudes into the cytoplasm functioning as a zinc sensor within the cell.

	Site A is located in both TMDs of the protein, while site C is located in the CTD, and site B is located at the junction of the domains join. Both TMD are composed of 6 helices, 4 of which (TM3-TM6) pivot about the ion binding site A. Zn<sup>2+</sup> binding at site C helps hold the CTD together and is thought to stabilize conformational changes in YiiP. YiiP has ~~a "Y" shape <scene name='75/756372/Newmainpic/1'> conformation</scene> with~~ two different functional conformations. An interlocked salt bridge connects the two domains with the Lys77 and the Asp207 from each monomer. This [https://en.wikipedia.org/wiki/Salt_bridge_(protein_and_supramolecular) salt bridge] acts as the hinge for the conformational changes that YiiP undergoes.		Site A is located in both TMDs of the protein, while site C is located in the CTD, and site B is located at the junction of the domains join. Both TMD are composed of 6 helices, 4 of which (TM3-TM6) pivot about the ion binding site A. Zn<sup>2+</sup> binding at site C helps hold the CTD together and is thought to stabilize conformational changes in YiiP. YiiP has two different functional conformations which dictates whether or not YiiP is open to the periplasm or the cytoplasm. An interlocked salt bridge connects the two domains with the Lys77 and the Asp207 from each monomer. This [https://en.wikipedia.org/wiki/Salt_bridge_(protein_and_supramolecular) salt bridge] acts as the hinge for the conformational changes that YiiP undergoes.