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6R5X

8-bladed beta-propeller formed by four 2-bladed fragments

Summary for 6R5X
Entry DOI10.2210/pdb6r5x/pdb
DescriptorWD-40 repeat protein (2 entities in total)
Functional Keywordsrepeat protein, fragment amplification, protein evolution, protein design, unknown function
Biological sourceNostoc punctiforme
Total number of polymer chains4
Total formula weight36215.71
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 citationAfanasieva, 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: 31613220
DOI: 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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