7AX0
Crystal structure of the computationally designed Scone-E protein co-crystallized with STA form a
Summary for 7AX0
Entry DOI | 10.2210/pdb7ax0/pdb |
Descriptor | SconeE, Keggin (STA), PHOSPHATE ION, ... (4 entities in total) |
Functional Keywords | beta-propeller, computational design, de novo protein |
Biological source | synthetic construct |
Total number of polymer chains | 1 |
Total formula weight | 43180.98 |
Authors | Mylemans, B.,Vandebroek, L.,Parac-Vogt, T.N.,Voet, A.R.D. (deposition date: 2020-11-09, release date: 2021-06-30, Last modification date: 2024-01-31) |
Primary citation | Mylemans, B.,Killian, T.,Vandebroek, L.,Van Meervelt, L.,Tame, J.R.H.,Parac-Vogt, T.N.,Voet, A.R.D. Crystal structures of Scone: pseudosymmetric folding of a symmetric designer protein. Acta Crystallogr D Struct Biol, 77:933-942, 2021 Cited by PubMed Abstract: Recent years have seen an increase in the development of computational proteins, including symmetric ones. A ninefold-symmetric β-propeller protein named Cake has recently been developed. Here, attempts were made to further engineer this protein into a threefold-symmetric nine-bladed propeller using computational design. Two nine-bladed propeller proteins were designed, named Scone-E and Scone-R. Crystallography, however, revealed the structure of both designs to adopt an eightfold conformation with distorted termini, leading to a pseudo-symmetric protein. One of the proteins could only be crystallized upon the addition of a polyoxometalate, highlighting the usefulness of these molecules as crystallization additives. PubMed: 34196619DOI: 10.1107/S2059798321005787 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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