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 which supported 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. The energy for inducing the conformation change from inward to outward is postulated to come from the binding energy of each substrate. The binding of Zn<sup>2+</sup> favors the outward-facing conformation, but the outward facing conformation does not favor the binding of Zn<sup>2+</sup>. The same is observed with the inward-facing conformation and H<sup>+</sup>. Although YiiP exists as a homodimer both monomers can undergo conformation change independent of one other to produce the alternating access mechanism. The main driving force behind exporting Zn<sup>2+</sup> from the cytoplasm is the proton motive force. | 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 which is supported 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. The energy for inducing the conformation change from inward to outward is postulated to come from the binding energy of each substrate. The binding of Zn<sup>2+</sup> favors the outward-facing conformation, but the outward facing conformation does not favor the binding of Zn<sup>2+</sup>. The same is observed with the inward-facing conformation and H<sup>+</sup>. Although YiiP exists as a homodimer both monomers can undergo conformation change independent of one other to produce the alternating access mechanism. The main driving force behind exporting Zn<sup>2+</sup> from the cytoplasm is the proton motive force. | ||
===Zn Induced Conformation Change=== | ===Zn Induced Conformation Change=== | ||
Revision as of 17:27, 29 March 2017
Zn Transporter YiiPZn Transporter YiiP
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. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue. OrganismThis protein is found in E. coli StructureYiiP is a homodimer with transmembrane (TMD) and C-terminal (CTD) domains that are connected via a charge interlocking mechanism located on a flexible loop. There are 3 Zn2+ binding sites per unit of homodimer. Site A is located in the TMD, site C is located in the CTD, and site B is located at the junction of the domains join. Both TMD are composed of 6 helices, 4 of which (TM1,TM2,TM4,TM5) form a pore in which Zn2+ and H+ can reach binding Site A. Zn2+ binding at site C helps hold the CTD together and is thought to stabilize conformational changes in YiiP. Mechanism of TransportYiiP's ability to export Zn2+ from the cytoplasm is best described as an alternating access mechanism with Zn2+/H+ antiport. YiiP has 2 major structural conformations which is supported 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. The energy for inducing the conformation change from inward to outward is postulated to come from the binding energy of each substrate. The binding of Zn2+ favors the outward-facing conformation, but the outward facing conformation does not favor the binding of Zn2+. The same is observed with the inward-facing conformation and H+. Although YiiP exists as a homodimer both monomers can undergo conformation change independent of one other to produce the alternating access mechanism. The main driving force behind exporting Zn2+ from the cytoplasm is the proton motive force. Zn Induced Conformation ChangeAllosteric InhibitionZn binding to Active Site C causes a conformation change that reduces the affinity for Zn at Active Site A. Structural highlightsThis is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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ReferencesReferences
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644