4DXO

Crystal Structure of a reconstructed Kaede-type Red Fluorescent Protein, LEA X(6)

4DXO の概要

• エントリーDOI: 10.2210/pdb4dxo/pdb
• 関連するPDBエントリー: 4DXI 4DXM 4DXN 4DXP 4DXQ
• 分子名称: LEA X(6) GFP-LIKE PROTEINS, SODIUM ION (3 entities in total)
• 機能のキーワード: beta barrel, luminescent protein
• 由来する生物種: Synthetic Construct (artificial)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26422.01

構造登録者

Kim, H.,Fromme, R.,Wachter, R.M. (登録日: 2012-02-27, 公開日: 2013-02-27, 最終更新日: 2024-11-20)

主引用文献

Kim, H.,Zou, T.,Modi, C.,Dorner, K.,Grunkemeyer, T.J.,Chen, L.,Fromme, R.,Matz, M.V.,Ozkan, S.B.,Wachter, R.M.
A hinge migration mechanism unlocks the evolution of green-to-red photoconversion in GFP-like proteins.
Structure, 23:34-43, 2015

PubMed Abstract: In proteins, functional divergence involves mutations that modify structure and dynamics. Here we provide experimental evidence for an evolutionary mechanism driven solely by long-range dynamic motions without significant backbone adjustments, catalytic group rearrangements, or changes in subunit assembly. Crystallographic structures were determined for several reconstructed ancestral proteins belonging to a GFP class frequently employed in superresolution microscopy. Their chain flexibility was analyzed using molecular dynamics and perturbation response scanning. The green-to-red photoconvertible phenotype appears to have arisen from a common green ancestor by migration of a knob-like anchoring region away from the active site diagonally across the β barrel fold. The allosterically coupled mutational sites provide active site conformational mobility via epistasis. We propose that light-induced chromophore twisting is enhanced in a reverse-protonated subpopulation, activating internal acid-base chemistry and backbone cleavage to enlarge the chromophore. Dynamics-driven hinge migration may represent a more general platform for the evolution of novel enzyme activities.

PubMed: 25565105
DOI: 10.1016/j.str.2014.11.011

実験手法

X-RAY DIFFRACTION (2.5 Å)