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<scene name='69/694234/3h90/1'>3h90</scene> is an integral membrane protein of the E. coli bacteria that regulates the import and export of Zn²⁺.

[[Image:Yiip_Electrostatic.png|250px|left|thumb|Electrostatics]]<scene name='69/694234/Electrostatic/1'>Charge distribution</scene> along the exterior surface of the protein is primarily neutral for the TMDs, but transitions to positive near the location of the charge interlock and interior side of the cell membrane. This positive section is characteristic of trans-membrane proteins as a means of achieving proper orientation. Binding sites A, B, and C, as well as the CTDs of both monomers, all possess a high negative charge relative to the other charges present, facilitating the binding and releasing of Zn²⁺ ions. The two CTDs are held together by the charge interlock and hydrophobic interactions of the TMDs despite their electrostatic repulsion. Upon the release of Zn²⁺ ions, the CTDs undergo electronegativity alterations, forcing the two domains apart.