Sandbox Reserved 1066: Difference between revisions
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==Zn Transporter YiiP== | ==Zn<sup>2+</sup> Transporter YiiP== | ||
<StructureSection load='3h90' size='340' side='right' caption='Zn Transporter' scene=''> | <StructureSection load='3h90' size='340' side='right' caption='Zn Transporter' scene=''> | ||
This is a default text for your page '''Kyle Colston/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page '''Kyle Colston/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
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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. | ||
===Zn Induced Conformation Change=== | ===Zn<sup>2+</sup> Induced Conformation Change=== | ||
Conformation changes occur in the TMD and CTD, both of which are heavily influenced by the presence of Zn<sup>2+</sup>. Both of these conformation changes are focused around the charge interlocking mechanism that holds the dimer together. This is because a flexible loop that likes the CTD and the TMD which acts as a hinge for | Conformation changes occur in the TMD and CTD, both of which are heavily influenced by the presence of Zn<sup>2+</sup>. Both of these conformation changes are focused around the charge interlocking mechanism that holds the dimer together. This is because a flexible loop that likes the CTD and the TMD which acts as a hinge for | ||
