6R5X
8-bladed beta-propeller formed by four 2-bladed fragments
Summary for 6R5X
| Entry DOI | 10.2210/pdb6r5x/pdb |
| Descriptor | WD-40 repeat protein (2 entities in total) |
| Functional Keywords | repeat protein, fragment amplification, protein evolution, protein design, unknown function |
| Biological source | Nostoc punctiforme |
| Total number of polymer chains | 4 |
| Total formula weight | 36215.71 |
| Authors | Martin, J.,Lupas, A.N.,Hartmann, M.D. (deposition date: 2019-03-25, release date: 2019-11-13, Last modification date: 2024-01-24) |
| Primary citation | Afanasieva, E.,Chaudhuri, I.,Martin, J.,Hertle, E.,Ursinus, A.,Alva, V.,Hartmann, M.D.,Lupas, A.N. Structural diversity of oligomeric beta-propellers with different numbers of identical blades. Elife, 8:-, 2019 Cited by PubMed Abstract: β-Propellers arise through the amplification of a supersecondary structure element called a blade. This process produces toroids of between four and twelve repeats, which are almost always arranged sequentially in a single polypeptide chain. We found that new propellers evolve continuously by amplification from single blades. We therefore investigated whether such nascent propellers can fold as homo-oligomers before they have been fully amplified within a single chain. One- to six-bladed building blocks derived from two seven-bladed WD40 propellers yielded stable homo-oligomers with six to nine blades, depending on the size of the building block. High-resolution structures for tetramers of two blades, trimers of three blades, and dimers of four and five blades, respectively, show structurally diverse propellers and include a novel fold, highlighting the inherent flexibility of the WD40 blade. Our data support the hypothesis that subdomain-sized fragments can provide structural versatility in the evolution of new proteins. PubMed: 31613220DOI: 10.7554/eLife.49853 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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