2RLI

Solution structure of Cu(I) human Sco2

Summary for 2RLI

• Entry DOI: 10.2210/pdb2rli/pdb
• Descriptor: SCO2 protein homolog, mitochondrial, COPPER (I) ION (2 entities in total)
• Functional Keywords: copper protein, thioredoxin fold, metal transport, structural genomics, spine2-complexes, structural proteomics in europe, spine, structural proteomics in europe 2, spine-2
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion: O43819
• Total number of polymer chains: 1
• Total formula weight: 19556.37

Authors

Banci, L.,Bertini, I.,Ciofi-baffoni, S.,Gerothanassis, I.P.,Leontari, I.,Martinelli, M.,Wang, S.,Structural Proteomics in Europe (SPINE),Structural Proteomics in Europe 2 (SPINE-2) (deposition date: 2007-07-11, release date: 2007-08-28, Last modification date: 2024-05-29)

Primary citation

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Gerothanassis, I.P.,Leontari, I.,Martinelli, M.,Wang, S.
A Structural Characterization of Human SCO2
Structure, 15:1132-1140, 2007

PubMed Abstract: Human Sco2 is a mitochondrial membrane-bound protein involved in copper supply for the assembly of cytochrome c oxidase in eukaryotes. Its precise action is not yet understood. We report here a structural and dynamic characterization by NMR of the apo and copper(I) forms of the soluble fragment. The structural and metal binding features of human Cu(I)Sco2 are similar to the more often studied Sco1 homolog, although the dynamic properties and the conformational disorder are quite different when the apo forms and the copper(I)-loaded forms of the two proteins are compared separately. Such differences are accounted for in terms of the different physicochemical properties in strategic protein locations. The misfunction of the known pathogenic mutations is discussed on the basis of the obtained structure.

PubMed: 17850752
DOI: 10.1016/j.str.2007.07.011

Experimental method

SOLUTION NMR