Sandbox Reserved 1069: Difference between revisions

YiiP is a homodimer [https://en.wikipedia.org/wiki/Protein_dimer (protein dimer)], with each monomer consisting of 238 residues with TransMembrane (<scene name='69/694236/Realtmd1/1'>TMD</scene>) and C-Terminal (<scene name='69/694236/Realctd1/1'>CTD</scene>) domains (colored blue) that are connected via a charge interlocking mechanism located on a flexible loop. In total, the Yiip protein has three Zn²⁺ <scene name='69/694236/Bindingsiteswcolor/2'>binding sites</scene>, site A, B, and C. Site A is located in the <scene name='69/694236/Bindingsiteswcolor/3'>TMD</scene> of the protein, highlighted in purple, site C is located in the <scene name='69/694236/Bindingsiteswcolor/4'>CTD</scene>, now seen in purple, and site B is located at the junction of the two domains. The TMD, where Zn²⁺ binding site A resides, consists of 6 transmembrane (TM) helices, 4 of which, <scene name='69/694236/Tmlabels/1'>TM1,TM2,TM4, and TM5</scene> (labeled on only one monomer, but present on both), pivot about the ion binding site A. The remaining two helices, <scene name='69/694236/Tm3tm6/2'>TM3 and TM6</scene>, are oriented <scene name='69/694236/Tm3tm6antiparallel/1'>antiparallel</scene> to the bundle. Movement of these helices plays a role in the function of Zn²⁺ transport.