6R60

asymmetric antiparallel assembly of two 5-bladed beta-propeller fragments

6R60 の概要

• エントリーDOI: 10.2210/pdb6r60/pdb
• 分子名称: WD-40 repeat protein (2 entities in total)
• 機能のキーワード: repeat protein, fragment amplification, protein evolution, protein design, wd40, unknown function
• 由来する生物種: Nostoc punctiforme
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 88533.01

構造登録者

Afanasieva, E.,Lupas, A.N.,Hartmann, M.D. (登録日: 2019-03-26, 公開日: 2019-11-13, 最終更新日: 2024-01-24)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (1.75 Å)