5HZT
Crystal structure of Dronpa-Cu2+
Summary for 5HZT
Entry DOI | 10.2210/pdb5hzt/pdb |
Related | 2GX2 5HZS 5HZU |
Descriptor | Fluorescent protein Dronpa, COPPER (II) ION (3 entities in total) |
Functional Keywords | fluorescent protein, luminescent protein |
Biological source | Echinophyllia sp. SC22 |
Total number of polymer chains | 12 |
Total formula weight | 297382.52 |
Authors | Hwang, K.Y.,Nam, K.H. (deposition date: 2016-02-03, release date: 2017-03-15, Last modification date: 2024-10-23) |
Primary citation | Kim, I.J.,Kim, S.,Park, J.,Eom, I.,Kim, S.,Kim, J.H.,Ha, S.C.,Kim, Y.G.,Hwang, K.Y.,Nam, K.H. Crystal structures of Dronpa complexed with quenchable metal ions provide insight into metal biosensor development FEBS Lett., 590:2982-2990, 2016 Cited by PubMed Abstract: Many fluorescent proteins (FPs) show fluorescence quenching by specific metal ions, which can be applied towards metal biosensor development. In this study, we investigated the significant fluorescence quenching of Dronpa by Co(2+) and Cu(2+) ions. Crystal structures of Co(2+) -, Ni(2+) - and Cu(2+) -bound Dronpa revealed previously unseen, unique, metal-binding sites for fluorescence quenching. These metal ions commonly interact with surface-exposed histidine residues (His194-His210 and His210-His212), and interact indirectly with chromophores. Structural analysis of the Co(2+) - and Cu(2+) - binding sites of Dronpa provides insight into FP-based metal biosensor engineering. PubMed: 27433793DOI: 10.1002/1873-3468.12316 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.84 Å) |
Structure validation
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