4MR1
X-ray structure of the adduct between hen egg white lysozyme and cis-diamminediiodoplatinum(II)
Summary for 4MR1
| Entry DOI | 10.2210/pdb4mr1/pdb |
| Descriptor | Lysozyme C, cis-diamino(diiodo)platinum, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | c-type lysozyme/alpha-lactalbumin family, hydrolase |
| Biological source | Gallus gallus (chicken) |
| Cellular location | Secreted: P00698 |
| Total number of polymer chains | 1 |
| Total formula weight | 14905.99 |
| Authors | Merlino, A. (deposition date: 2013-09-17, release date: 2014-06-04, Last modification date: 2024-11-20) |
| Primary citation | Messori, L.,Marzo, T.,Gabbiani, C.,Valdes, A.A.,Quiroga, A.G.,Merlino, A. Peculiar features in the crystal structure of the adduct formed between cis-PtI2(NH3)2 and hen egg white lysozyme. Inorg.Chem., 52:13827-13829, 2013 Cited by PubMed Abstract: The reactivity of cis-diamminediiodidoplatinum(II), cis-PtI2(NH3)2, the iodo analogue of cisplatin, with hen egg white lysozyme (HEWL) was investigated by electrospray ionization mass spectrometry and X-ray crystallography. Interestingly, the study compound forms a stable 1:1 protein adduct for which the crystal structure was solved at 1.99 Å resolution. In this adduct, the Pt(II) center, upon release of one ammonia ligand, selectively coordinates to the imidazole of His15. Both iodide ligands remain bound to platinum, with this being a highly peculiar and unexpected feature. Notably, two equivalent modes of Pt(II) binding are possible that differ only in the location of I atoms with respect to ND1 of His15. The structure of the adduct was compared with that of HEWL-cisplatin, previously described; differences are stressed and their important mechanistic implications discussed. PubMed: 24256441DOI: 10.1021/ic402611m PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.99 Å) |
Structure validation
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