LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| 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 flexneri has been determined. The fold has been classed as a ferredoxin-like α-β sandwich, having a beta-alpha β-β α-β architecture, with the two α-helices overlaying a four-stranded anti-parallel β-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 |
