6Z5G
The RSL - sulfonato-calix[8]arene complex, I23 form, citrate pH 4.0, solved by S-SAD
Summary for 6Z5G
| Entry DOI | 10.2210/pdb6z5g/pdb |
| Related | 6STH |
| Descriptor | Fucose-binding lectin protein, GLYCEROL, beta-D-fructopyranose, ... (5 entities in total) |
| Functional Keywords | calixarene, protein framework, cage, crystal engineering, molecular glue, synthetic receptor, macrocycle, biomaterial, sugar binding protein |
| Biological source | Ralstonia solanacearum |
| Total number of polymer chains | 1 |
| Total formula weight | 13076.87 |
| Authors | Engilberge, S.,Ramberg, K.,Crowley, P.B. (deposition date: 2020-05-26, release date: 2021-04-14, Last modification date: 2024-01-24) |
| Primary citation | Ramberg, K.O.,Engilberge, S.,Skorek, T.,Crowley, P.B. Facile Fabrication of Protein-Macrocycle Frameworks. J.Am.Chem.Soc., 143:1896-1907, 2021 Cited by PubMed Abstract: Precisely defined protein aggregates, as exemplified by crystals, have applications in functional materials. Consequently, engineered protein assembly is a rapidly growing field. Anionic calix[n]arenes are useful scaffolds that can mold to cationic proteins and induce oligomerization and assembly. Here, we describe protein-calixarene composites obtained via cocrystallization of commercially available sulfonato-calix[8]arene () with the symmetric and "neutral" protein RSL. Cocrystallization occurred across a wide range of conditions and protein charge states, from pH 2.2-9.5, resulting in three crystal forms. Cationization of the protein surface at pH ∼ 4 drives calixarene complexation and yielded two types of porous frameworks with pore diameters >3 nm. Both types of framework provide evidence of protein encapsulation by the calixarene. Calixarene-masked proteins act as nodes within the frameworks, displaying octahedral-type coordination in one case. The other framework formed millimeter-scale crystals within hours, without the need for precipitants or specialized equipment. NMR experiments revealed macrocyclemodulated side chain p values and suggested a mechanism for pH-triggered assembly. The same low pH framework was generated at high pH with a permanently cationic arginine-enriched RSL variant. Finally, in addition to protein framework fabrication, enables structure determination. PubMed: 33470808DOI: 10.1021/jacs.0c10697 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.278 Å) |
Structure validation
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