6I3A
Crystal structure of v22Pizza6-AYW, a circularly permuted designer protein
Summary for 6I3A
| Entry DOI | 10.2210/pdb6i3a/pdb |
| Descriptor | v22Pizza6-AYW, BROMIDE ION (3 entities in total) |
| Functional Keywords | circularly permuted designer protein, artificial protein, beta-propeller, pizza, de novo protein |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 26359.78 |
| Authors | Mylemans, B.,Noguchi, H.,Deridder, E.,Voet, A.R.D. (deposition date: 2018-11-05, release date: 2019-11-20, Last modification date: 2024-01-24) |
| Primary citation | Mylemans, B.,Noguchi, H.,Deridder, E.,Lescrinier, E.,Tame, J.R.H.,Voet, A.R.D. Influence of circular permutations on the structure and stability of a six-fold circular symmetric designer protein. Protein Sci., 2020 Cited by PubMed Abstract: The β-propeller fold is adopted by a sequentially diverse family of repeat proteins with apparent rotational symmetry. While the structure is mostly stabilized by hydrophobic interactions, an additional stabilization is provided by hydrogen bonds between the N-and C-termini, which are almost invariably part of the same β-sheet. This feature is often referred to as the "Velcro" closure. The positioning of the termini within a blade is variable and depends on the protein family. In order to investigate the influence of this location on protein structure, folding and stability, we created different circular permutants, and a circularized version, of the designer propeller protein named Pizza. This protein is perfectly symmetrical, possessing six identical repeats. While all mutants adopt the same structure, the proteins lacking the "Velcro" closure were found to be significantly less resistant to thermal and chemical denaturation. This could explain why such proteins are rarely observed in nature. Interestingly the most common "Velcro" configuration for this protein family was not the most stable among the Pizza variants tested. The circularized version shows dramatically improved stability, which could have implications for future applications. PubMed: 33006397DOI: 10.1002/pro.3961 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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