8XH1
Orthorhombic crystal structure of green fluorescent protein nowGFP at pH 9.0
Summary for 8XH1
| Entry DOI | 10.2210/pdb8xh1/pdb |
| Related | 8XH0 |
| Descriptor | nowGFP, GLYCEROL (3 entities in total) |
| Functional Keywords | green fluorescent protein, crystal polymorphism, fluorescent protein |
| Biological source | synthetic construct |
| Total number of polymer chains | 2 |
| Total formula weight | 53512.33 |
| Authors | |
| Primary citation | Kim, J.K.,Jeong, H.,Seo, J.,Kim, S.,Kim, K.H.,Min, D.,Kim, C.U. Comparison of two crystal polymorphs of NowGFP reveals a new conformational state trapped by crystal packing. Acta Crystallogr D Struct Biol, 80:686-698, 2024 Cited by PubMed Abstract: Crystal polymorphism serves as a strategy to study the conformational flexibility of proteins. However, the relationship between protein crystal packing and protein conformation often remains elusive. In this study, two distinct crystal forms of a green fluorescent protein variant, NowGFP, are compared: a previously identified monoclinic form (space group C2) and a newly discovered orthorhombic form (space group P222). Comparative analysis reveals that both crystal forms exhibit nearly identical linear assemblies of NowGFP molecules interconnected through similar crystal contacts. However, a notable difference lies in the stacking of these assemblies: parallel in the monoclinic form and perpendicular in the orthorhombic form. This distinct mode of stacking leads to different crystal contacts and induces structural alteration in one of the two molecules within the asymmetric unit of the orthorhombic crystal form. This new conformational state captured by orthorhombic crystal packing exhibits two unique features: a conformational shift of the β-barrel scaffold and a restriction of pH-dependent shifts of the key residue Lys61, which is crucial for the pH-dependent spectral shift of this protein. These findings demonstrate a clear connection between crystal packing and alternative conformational states of proteins, providing insights into how structural variations influence the function of fluorescent proteins. PubMed: 39222305DOI: 10.1107/S2059798324008246 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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