8ZBO
Crystal structure of the biphotochromic fluorescent protein moxSAASoti (F97M variant) in its green on-state
Summary for 8ZBO
| Entry DOI | 10.2210/pdb8zbo/pdb |
| Descriptor | F97M variant of the biphotochromic fluorescent protein moxSAASoti, NITRATE ION, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | moxsaasoti, point mutant, fluorescent protein, chromophore, msaasoti, saasoti, biphotochromic |
| Biological source | Stylocoeniella armata |
| Total number of polymer chains | 2 |
| Total formula weight | 51001.39 |
| Authors | Boyko, K.M.,Matyuta, I.O.,Marynich, N.K.,Minyaev, M.E.,Khadiyatova, A.A.,Popov, V.O.,Savitsky, A.P. (deposition date: 2024-04-26, release date: 2024-06-12, Last modification date: 2024-11-13) |
| Primary citation | Marynich, N.K.,Boyko, K.M.,Matyuta, I.O.,Minyaev, M.E.,Khadiyatova, A.A.,Popov, V.O.,Savitsky, A.P. Single-point substitution F97M leads to in cellulo crystallization of the biphotochromic protein moxSAASoti. Biochem.Biophys.Res.Commun., 732:150419-150419, 2024 Cited by PubMed Abstract: To enhance the photoconversion performance of biphotochromic moxSAASoti protein, a substitution F97 M was introduced. In addition to enhancing the target properties, this substitution also resulted in the crystallization of the recombinant protein within living HeLa cells (also referred to as in cellulo crystallization). The phenomenon of protein crystallization in living cells is not unique, yet the mechanisms and application of in cellulo crystallization remain significant for further research. However, in cellulo crystallization is atypical for fluorescent proteins and detrimental for their biotechnological application. The objective of this study was to elucidate the underlying mechanisms responsible for the crystallization of moxSAASotiin cellulo. For this purpose, the crystal structure of the green form of biphotochromic protein moxSAASoti was determined at high resolution, which surprisingly has a space group, different from those of parent mSAASoti. The analysis provided allowed to propose a mechanism of new crystal contacts formation, which might be a cause of in cellulo protein crystallization. PubMed: 39032411DOI: 10.1016/j.bbrc.2024.150419 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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