4NY5
X-ray structure of the adduct formed between hen egg white lysozyme and NAMI-A
Summary for 4NY5
| Entry DOI | 10.2210/pdb4ny5/pdb |
| Related | 4J1A 4J1B |
| Descriptor | Lysozyme C, RUTHENIUM ION, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | hydrolase, o-glycosyl |
| Biological source | Gallus gallus (bantam,chickens) |
| Total number of polymer chains | 1 |
| Total formula weight | 14627.20 |
| Authors | Messori, L.,Merlino, A. (deposition date: 2013-12-10, release date: 2014-03-26, Last modification date: 2024-11-27) |
| Primary citation | Messori, L.,Merlino, A. Ruthenium metalation of proteins: the X-ray structure of the complex formed between NAMI-A and hen egg white lysozyme. Dalton Trans, 43:6128-6131, 2014 Cited by PubMed Abstract: A crystallographic study of the adduct formed between hen egg white lysozyme (HEWL) and NAMI-A, an established ruthenium(III) anticancer agent in clinical trials, is presented here. The X-ray structure reveals that NAMI-A coordinates the protein, as a naked ruthenium ion, at two distinct sites (namely Asp101 or Asp119) after releasing all its original ligands (DMSO, imidazole and Cl(-)). Structural data of the HEWL/NAMI-A adduct are compared with those previously obtained for the HEWL adduct of AziRu, a NAMI-A analogue bearing a pyridine in place of imidazole. The present results further support the view that NAMI-A exerts its biological effects acting as a classical "prodrug" first undergoing activation and then causing extensive metalation of relevant protein targets. It is also proposed that the original Ru-ligands, although absent in the final adduct, play a major role in directing the ruthenium center to its ultimate anchoring site on the protein surface. PubMed: 24553967DOI: 10.1039/c3dt53582g PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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