7TA8
NMR structure of crosslinked cyclophilin A
Summary for 7TA8
| Entry DOI | 10.2210/pdb7ta8/pdb |
| NMR Information | BMRB: 30977 |
| Descriptor | Peptidyl-prolyl cis-trans isomerase A (1 entity in total) |
| Functional Keywords | isomerase, side chain crosslink |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 18065.50 |
| Authors | Lu, M.,Toptygin, D.,Xiang, Y.,Shi, Y.,Schwieters, C.D.,Lipinski, E.C.,Ahn, J.,Byeon, I.-J.L.,Gronenborn, A.M. (deposition date: 2021-12-20, release date: 2022-06-01, Last modification date: 2024-10-30) |
| Primary citation | Lu, M.,Toptygin, D.,Xiang, Y.,Shi, Y.,Schwieters, C.D.,Lipinski, E.C.,Ahn, J.,Byeon, I.L.,Gronenborn, A.M. The Magic of Linking Rings: Discovery of a Unique Photoinduced Fluorescent Protein Crosslink. J.Am.Chem.Soc., 144:10809-10816, 2022 Cited by PubMed Abstract: Fluorosubstituted tryptophans serve as valuable probes for fluorescence and nuclear magnetic resonance (NMR) studies of proteins. Here, we describe an unusual photoreactivity introduced by replacing the single tryptophan in cyclophilin A with 7-fluoro-tryptophan. UV exposure at 282 nm defluorinates 7-fluoro-tryptophan and crosslinks it to a nearby phenylalanine, generating a bright fluorophore. The crosslink-containing fluorescent protein possesses a large quantum yield of ∼0.40 with a fluorescence lifetime of 2.38 ns. The chemical nature of the crosslink and the three-dimensional protein structure were determined by mass spectrometry and NMR spectroscopy. To the best of our knowledge, this is the first report of a Phe-Trp crosslink in a protein. Our finding may break new ground for developing novel fluorescence probes and for devising new strategies to exploit aromatic crosslinks in proteins. PubMed: 35574633DOI: 10.1021/jacs.2c02054 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
