6V51
Spin-labeled T4 Lysozyme (9/131FnbY)-(4-Amino-TEMPO)
Summary for 6V51
| Entry DOI | 10.2210/pdb6v51/pdb |
| Descriptor | Endolysin, 4-amino-2,2,6,6-tetramethylpiperidin-1-ol (3 entities in total) |
| Functional Keywords | lysozyme, hydrolase |
| Biological source | Enterobacteria phage T4 |
| Total number of polymer chains | 1 |
| Total formula weight | 19098.97 |
| Authors | Liu, J.,Morizumi, T.,Ou, W.L.,Wang, L.,Ernst, O.P. (deposition date: 2019-12-02, release date: 2020-10-07, Last modification date: 2023-10-11) |
| Primary citation | Liu, J.,Cheng, R.,Van Eps, N.,Wang, N.,Morizumi, T.,Ou, W.L.,Klauser, P.C.,Rozovsky, S.,Ernst, O.P.,Wang, L. Genetically Encoded Quinone Methides Enabling Rapid, Site-Specific, and Photocontrolled Protein Modification with Amine Reagents. J.Am.Chem.Soc., 142:17057-17068, 2020 Cited by PubMed Abstract: Site-specific modification of proteins with functional molecules provides powerful tools for researching and engineering proteins. Here we report a new chemical conjugation method which photocages highly reactive but chemically selective moieties, enabling the use of protein-inert amines for selective protein modification. New amino acids FnbY and FmnbY, bearing photocaged quinone methides (QMs), were genetically incorporated into proteins. Upon light activation, they generated highly reactive QM, which rapidly reacted with amine derivatives. This method features a rare combination of desired properties including fast kinetics, small and stable linkage, compatibility with low temperature, photocontrollability, and widely available reagents. Moreover, labeling via FnbY occurs on the β-carbon, affording the shortest linkage to protein backbone which is essential for advanced studies involving orientation and distance. We installed various functionalities onto proteins and attached a spin label as close as possible to the protein backbone, achieving high resolution in double electron-electron paramagnetic resonance distance measurements. PubMed: 32915556DOI: 10.1021/jacs.0c06820 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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