1M42
Solution structure of apoCopC from Pseudomonas syringae
Summary for 1M42
| Entry DOI | 10.2210/pdb1m42/pdb |
| Descriptor | Copper resistance protein C (1 entity in total) |
| Functional Keywords | cupredoxins, copper trafficking, metal binding protein |
| Biological source | Pseudomonas syringae |
| Cellular location | Periplasm: P12376 |
| Total number of polymer chains | 1 |
| Total formula weight | 10547.08 |
| Authors | Arnesano, F.,Banci, L.,Bertini, I.,Thompsett, A.R. (deposition date: 2002-07-02, release date: 2002-11-06, Last modification date: 2024-05-22) |
| Primary citation | Arnesano, F.,Banci, L.,Bertini, I.,Thompsett, A.R. Solution structure of CopC: a cupredoxin-like protein involved in copper homeostasis Structure, 10:1337-1347, 2002 Cited by PubMed Abstract: The structure of the metal-free form of CopC, a protein involved in copper homeostasis, has been obtained. The fold is a Greek key beta barrel similar to that of functionally unrelated blue copper proteins but with important structural variations. The protein binds one equivalent of copper (II) with relatively high affinity and contains a cluster of conserved residues (His1, Glu27, Asp89, and His91) which could form a water-accessible metal binding site. The structure also reveals a loop containing the M(X)(n)M motif which is present in a number of proteins also involved in copper homeostasis. The present structure represents a link between copper-trafficking proteins and cupredoxins. Within a structural and genomic analysis, the role of CopC in copper trafficking is discussed. PubMed: 12377120DOI: 10.1016/S0969-2126(02)00858-4 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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