3RYM
Structure of Oxidized M98K mutant of Amicyanin
Summary for 3RYM
| Entry DOI | 10.2210/pdb3rym/pdb |
| Related | 1AAC 2OV0 3IE9 |
| Descriptor | Amicyanin, ZINC ION (3 entities in total) |
| Functional Keywords | type i blue copper protein, beta sandwich, electron transport, metal binding |
| Biological source | Paracoccus denitrificans |
| Cellular location | Periplasm: P22364 |
| Total number of polymer chains | 4 |
| Total formula weight | 46405.07 |
| Authors | Sukumar, N.,Davidson, V.L. (deposition date: 2011-05-11, release date: 2011-11-23, Last modification date: 2023-09-13) |
| Primary citation | Sukumar, N.,Choi, M.,Davidson, V.L. Replacement of the axial copper ligand methionine with lysine in amicyanin converts it to a zinc-binding protein that no longer binds copper. J.Inorg.Biochem., 105:1638-1644, 2011 Cited by PubMed Abstract: The mutation of the axial ligand of the type I copper protein amicyanin from Met to Lys results in a protein that is spectroscopically invisible and redox inactive. M98K amicyanin acts as a competitive inhibitor in the reaction of native amicyanin with methylamine dehydrogenase indicating that the M98K mutation has not affected the affinity for its natural electron donor. The crystal structure of M98K amicyanin reveals that its overall structure is very similar to native amicyanin but that the type I binding site is occupied by zinc. Anomalous difference Fourier maps calculated using the data collected around the absorption edges of copper and zinc confirm the presence of Zn(2+) at the type I site. The Lys98 NZ donates a hydrogen bond to a well-ordered water molecule at the type I site which enhances the ability of Lys98 to provide a ligand for Zn(2+). Attempts to reconstitute M98K apoamicyanin with copper resulted in precipitation of the protein. The fact that the M98K mutation generated such a selective zinc-binding protein was surprising as ligation of zinc by Lys is rare and this ligand set is unique for zinc. PubMed: 22071089DOI: 10.1016/j.jinorgbio.2011.08.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7039 Å) |
Structure validation
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