6533b86dfe1ef96bd12c9391
RESEARCH PRODUCT
false
Enrique Pérez-payáEnrique Pérez-payáIsmael MingarroErnest GiraltLola PeñarrubiaHelena MiraMarcelo J. KoganDavid SalomMarc MartinellVicent EsteveMarçal Vilarsubject
endocrine systembiologyfood and beverageschemistry.chemical_elementPlasmodesmabiology.organism_classificationCopperYeastMetallochaperonesCytosolProtein structurechemistryBiochemistryStructural BiologyArabidopsisBiophysicsPeptide sequencedescription
Background Arabidopsis thaliana copper metallochaperone CCH is a functional homologue of yeast antioxidant ATX1, involved in cytosolic copper transport. In higher plants, CCH has to be transported to specialised cells through plasmodesmata, being the only metallochaperone reported to date that leaves the cell where it is synthesised. CCH has two different domains, the N-terminal domain conserved among other copper-metallochaperones and a C-terminal domain absent in all the identified non-plant metallochaperones. The aim of the present study was the biochemical and biophysical characterisation of the C-terminal domain of the copper metallochaperone CCH.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2004-01-01 | BMC Structural Biology |