7OG7
Crystal structure of the copper chaperone NosL from Shewanella denitrificans
Summary for 7OG7
| Entry DOI | 10.2210/pdb7og7/pdb |
| Descriptor | NosL, COPPER (I) ION, ZINC ION, ... (5 entities in total) |
| Functional Keywords | copper chaperone, metal binding protein |
| Biological source | Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013) |
| Total number of polymer chains | 1 |
| Total formula weight | 20654.30 |
| Authors | Prasser, B.,Schoener, L.,Zhang, L.,Einsle, O. (deposition date: 2021-05-06, release date: 2021-07-07, Last modification date: 2024-06-19) |
| Primary citation | Prasser, B.,Schoner, L.,Zhang, L.,Einsle, O. The Copper Chaperone NosL Forms a Heterometal Site for Cu Delivery to Nitrous Oxide Reductase. Angew.Chem.Int.Ed.Engl., 60:18810-18814, 2021 Cited by PubMed Abstract: The final step of denitrification is the reduction of nitrous oxide (N O) to N , mediated by Cu-dependent nitrous oxide reductase (N OR). Its metal centers, Cu and Cu , are assembled through sequential provision of twelve Cu ions by a metallochaperone that forms part of a nos gene cluster encoding the enzyme and its accessory factors. The chaperone is the nosL gene product, an 18 kDa lipoprotein predicted to reside in the outer membrane of Gram-negative bacteria. In order to better understand the assembly of N OR, we have produced NosL from Shewanella denitrificans and determined the structure of the metal-loaded chaperone by X-ray crystallography. The protein assembled a heterodinuclear metal site consisting of Zn and Cu , as evidenced by anomalous X-ray scattering. While only Cu is delivered to the enzyme, the stabilizing presence of Zn is essential for the functionality and structural integrity of the chaperone. PubMed: 34171184DOI: 10.1002/anie.202106348 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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