Summary for 7BK5
| Entry DOI | 10.2210/pdb7bk5/pdb |
| Descriptor | Putative copper resistance protein, COPPER (II) ION, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | copper binding, copper transport, metal binding protein |
| Biological source | Pseudomonas fluorescens (strain SBW25) |
| Total number of polymer chains | 1 |
| Total formula weight | 10352.59 |
| Authors | Muderspach, S.J.,Ipsen, J.,Rollan, C.H.,Bertelsen, A.B.,Norholm, M.H.H.,Johansen, K.S.,Lo Leggio, L. (deposition date: 2021-01-15, release date: 2021-07-07, Last modification date: 2024-01-31) |
| Primary citation | Ipsen, J.O.,Hernandez-Rollan, C.,Muderspach, S.J.,Brander, S.,Bertelsen, A.B.,Jensen, P.E.,Norholm, M.H.H.,Lo Leggio, L.,Johansen, K.S. Copper binding and reactivity at the histidine brace motif: insights from mutational analysis of the Pseudomonas fluorescens copper chaperone CopC. Febs Lett., 595:1708-1720, 2021 Cited by PubMed Abstract: The histidine brace (His-brace) is a copper-binding motif that is associated with both oxidative enzymes and proteinaceous copper chaperones. Here, we used biochemical and structural methods to characterize mutants of a His-brace-containing copper chaperone from Pseudomonas fluorescens (PfCopC). A total of 15 amino acid variants in primary and second-sphere residues were produced and characterized in terms of their copper binding and redox properties. PfCopC has a very high affinity for Cu(II) and also binds Cu(I). A high reorganization barrier likely prevents redox cycling and, thus, catalysis. In contrast, mutations in the conserved second-sphere Glu27 enable slow oxidation of ascorbate. The crystal structure of the variant E27A confirmed copper binding at the His-brace. Unexpectedly, Asp83 at the equatorial position was shown to be indispensable for Cu(II) binding in the His-brace of PfCopC. A PfCopC mutant that was designed to mimic the His-brace from lytic polysaccharide monooxygenase-like family X325 did not bind Cu(II), but was still able to bind Cu(I). These results highlight the importance of the proteinaceous environment around the copper His-brace for reactivity and, thus, the difference between enzyme and chaperone. PubMed: 33896006DOI: 10.1002/1873-3468.14092 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.54 Å) |
Structure validation
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