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[[Image:YiiP_Mechanism.png|300px|right|thumb| Figure 5. General mechanism that YiiP uses to transport Zn2+ from the cytoplasm to the periplasm. This mechanism involves 2 major conformations; the inward-facing conformation (A & B) and the outward-facing conformation (C & D). Helices TM1, TM2, TM4, and TM5 (blue) are shown pivoting relative to helices TM3 & TM6 (red). The CTD (yellow) does not move during this conformation change as it it held together tightly by binding Zn<sup>2+</sup>.]]
[[Image:YiiP_Mechanism.png|300px|right|thumb| Figure 5. General mechanism that YiiP uses to transport Zn2+ from the cytoplasm to the periplasm. This mechanism involves 2 major conformations; the inward-facing conformation (A & B) and the outward-facing conformation (C & D). Helices TM1, TM2, TM4, and TM5 (blue) are shown pivoting relative to helices TM3 & TM6 (red). The CTD (yellow) does not move during this conformation change as it it held together tightly by binding Zn<sup>2+</sup>.]]
YiiP's ability to export Zn<sup>2+</sup> from the cytoplasm is best described as an alternating access mechanism with Zn<sup>2+</sup>/H<sup>+</sup> antiport. YiiP has 2 major structural conformations as shown by the crystallized structures [http://proteopedia.org/wiki/index.php/3h90 3H90] and [http://proteopedia.org/wiki/index.php/3j1z 3J1Z] <ref>PMID:23341604</ref> (a YiiP homolog derived from ''Shewanella oneidensis''). 3H90 shows YiiP in its outward-facing conformation with Zn<sup>2+</sup> present and 3J1Z which shows the YiiP homolog in an inward-facing conformation where there is no Zn<sup>2+</sup> present.
YiiP's ability to export Zn<sup>2+</sup> from the cytoplasm is best described as an alternating access mechanism with Zn<sup>2+</sup>/H<sup>+</sup> antiport (Figure 5.). YiiP has 2 major structural conformations as shown by the crystallized structures [http://proteopedia.org/wiki/index.php/3h90 3H90] and [http://proteopedia.org/wiki/index.php/3j1z 3J1Z] <ref>PMID:23341604</ref> (a YiiP homolog derived from ''Shewanella oneidensis''). 3H90 shows YiiP in its outward-facing conformation with Zn<sup>2+</sup> present and 3J1Z which shows the YiiP homolog in an inward-facing conformation where there is no Zn<sup>2+</sup> present.
When YiiP is saturated with Zn<sup>2+</sup> it favors the <scene name='69/694236/Outward-facinggreen/1'>outward-facing conformation</scene> whereas when active sites are either empty or bound to H<sup>+</sup> the <scene name='69/694236/Inward-facinggreen/1'>inward-facing conformation</scene> is favored. This drives the export of Zn<sup>2+</sup> from the cytoplasm to the periplasm. Although YiiP exists as a homodimer both monomers can undergo conformation change independent of one other to  
When YiiP is saturated with Zn<sup>2+</sup> it favors the <scene name='69/694236/Outward-facinggreen/1'>outward-facing conformation</scene> whereas when active sites are either empty or bound to H<sup>+</sup> the <scene name='69/694236/Inward-facinggreen/1'>inward-facing conformation</scene> is favored. This drives the export of Zn<sup>2+</sup> from the cytoplasm to the periplasm. Although YiiP exists as a homodimer both monomers can undergo conformation change independent of one other to  
produce the alternating access mechanism.
produce the alternating access mechanism.

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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