Sandbox Reserved 1066

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.

Organism

This protein is found in E. coli

Structure

YiiP 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 Transport

Zn Induced Conformation Change

Allosteric Inhibition

Zn binding to Active Site C causes a conformation change that reduces the affinity for Zn at Active Site A.

Structural highlights

This 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.