Sandbox Reserved 1066: Difference between revisions
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==Mechanism of Transport== | ==Mechanism of Transport== | ||
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 3H90 and 3J1Z (a YiiP homolog derived from ''Shewanella oneidensis''). 3H90 shows YiiP in its outward-facing conformation and 3J1Z shows the YiiP homolog in an inward-facing conformation. | 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 [[3H90]] and [[3J1Z]] (a YiiP homolog derived from ''Shewanella oneidensis''). 3H90 shows YiiP in its outward-facing conformation and 3J1Z shows the YiiP homolog in an inward-facing conformation. | ||
When YiiP is saturated with Zn<sup>2+</sup> it seems to favor the perplasmic/outward-facing conformation whereas when active sites are either empty or bound to H<sup>+</sup> the inward facing conformation is favored. This drives the export of Zn<sup>2+</sup> from the cytoplasm and enhances the coupling of the proton-motive force. Although YiiP exists as a homodimer both monomers can undergo conformation change independent of one other to produce the alternating access mechanism. | When YiiP is saturated with Zn<sup>2+</sup> it seems to favor the perplasmic/outward-facing conformation whereas when active sites are either empty or bound to H<sup>+</sup> the inward facing conformation is favored. This drives the export of Zn<sup>2+</sup> from the cytoplasm and enhances the coupling of the proton-motive force. Although YiiP exists as a homodimer both monomers can undergo conformation change independent of one other to produce the alternating access mechanism. | ||
