1 Child Features
DB identifier | Type | Name |
---|---|---|
IPR011795 | Family | Mercuric transport protein periplasmic component |
Type: | Family | Name: | Mercuric transport protein periplasmic component/copper chaperone CopZ |
Description: | This entry includes a group of metal binding proteins, including copper chaperone CopZ [] and mercuric transport protein periplasmic component MerP. They both contain a heavy-metal-associated (HMA) domain. CopZ is a chaperone that serves for the intracellular sequestration and transport of Cu+. It delivers Cu+ to the copper-exporting P-type ATPase A (CopA)[].MerP is a mercury scavenger that specifically binds to one mercury ion and which passes it to the mercuric reductase (MerA) via the MerT protein. The structure of the mercuric ion-binding protein MerP from Shigella flexnerihas been determined. The fold has been classed as a ferredoxin-like alpha-beta sandwich, having a beta-alpha beta-beta alpha-beta architecture, with the two alpha-helices overlaying a four-stranded anti-parallel beta-sheet []. Structural differences between the reduced and mercury-bound forms of merP are localised to the metal-binding loop containing the consensus sequence GMTCXXC, the two cysteines of which are involved in bi-coordination of Hg2+[]. | Short Name: | MerP/CopZ |
DB identifier | Type | Name |
---|---|---|
IPR011795 | Family | Mercuric transport protein periplasmic component |