7CZ0
Crystal structure of a thermostable green fluorescent protein (TGP) with a synthetic nanobody (Sb92)
Summary for 7CZ0
| Entry DOI | 10.2210/pdb7cz0/pdb |
| Descriptor | Thermostable green fluorescent protein (TGP), Synthetic nanobody (Sybody) 92 recognizing the thermostable green fluorescent protein (TGP), GLYCEROL, ... (6 entities in total) |
| Functional Keywords | complex, gfp, nanobody, single-chain antibody, sybody, synthetic antibody, tgp, thermostable green fluorescent protein, fluorescent protein |
| Biological source | Galaxea fascicularis More |
| Total number of polymer chains | 8 |
| Total formula weight | 171451.55 |
| Authors | Cai, H.,Yao, H.,Li, T.,Hutter, C.,Tang, Y.,Li, Y.,Seeger, M.,Li, D. (deposition date: 2020-09-06, release date: 2021-09-08, Last modification date: 2026-07-01) |
| Primary citation | Yue, Z.,Li, Y.,Cai, H.,Yao, H.,Li, D.,Ni, A.,Li, T. Structure-based design of covalent nanobody binders for a thermostable green fluorescence protein. Acta Biochim.Biophys.Sin., 57:1363-1370, 2024 Cited by PubMed Abstract: The use of green fluorescence protein (GFP) has advanced numerous areas of life sciences. An ultra-thermostable GFP (TGP), engineered from a coral GFP, offers potential advantages over traditional jellyfish-derived GFP because of its high stability. However, owing to its later discovery, TGP lacks the extensive toolsets available for GFP, such as heavy chain-only antibody binders known as nanobodies. In this study, we report the crystal structure of TGP in complex with Sb92, a synthetic nanobody identified from a previous screening, revealing Sb92's precise three-dimensional epitope. This structural insight, alongside the previously characterized Sb44-TGP complex, allows us to rationally design disulfide bonds between the antigen and the antibody for tighter interactions. Using biochemical analysis, we identify two bridged complexes (TGP A18C-Sb44 V100C and TGP E118C-Sb92 S57C), with the TGP-Sb92 disulfide pair showing high resistance to reducing agents. Our study expands the toolkit available for TGP and should encourage its wider applications. PubMed: 39719878DOI: 10.3724/abbs.2024233 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.77 Å) |
Structure validation
Download full validation report
