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 (CTD) 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 CTD, 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 (CTD) 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 CTD, 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 (~~TM1,TM2,TM4,TM5~~) ~~form a pore in which Zn<sup>2+</sup> and H<sup>+</sup> can reach~~ 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 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.