Copper is one of the most important metal involed in multiple enzyme catalysed reactions as a cofactor. In living organisms its function is related to the redox property of the copper. However it is toxic at all co,ce,tration, from the lower to the higher, and it need to be strictly controled in living organisms by molecular mechanisms.[1]
Function
Multicopper oxidases are enzymes involved in copper homeostasis. Copper as many metal ions is used in multiple biological processes such as detoxification of oxygen free radicals and pigmentation. However copper present in a cell bot bounded to a protein if harmfull and can cause cellular damage. It need to be regulated.
Multicopper oxidase might also be involved in the regulation of metal transport.
Multicopper oxidases are abble to oxiise their substrate. They accept an electron in the and transfer it to the trinuclear copper centre. The dioxygen bind to the trinuclear center and recieve four electron. It is transformed into two molecules of water.[2] Three copper centres exist that can be differentiate spectroscopically: Type 1 or blue (), type 2 or normal (Cu1004) and type 3 or coupled binuclear (1002 and 1003).[3][4]
Disease
If the amino acids 500 and 501 are mutated from CH to SR, the residual activity and loss of resistance to copper. E. Coli die.
Relevance
Structural highlights
Multicopper Oxidase CueO 4e9s is a protein containing one chain with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: |  Figure 1: Acetate ion. [5] |
| Related: | 4e9p, 4e9q, 4e9r, 4e9t |
| Gene: | cueO, yacK, b0123, JW0119 (ECOLI) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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.
