1NWZ

PYP Ultra-high resolution structure of a Bacterial Photoreceptor

1NWZ の概要

• エントリーDOI: 10.2210/pdb1nwz/pdb
• 分子名称: Photoactive yellow protein, 4'-HYDROXYCINNAMIC ACID (3 entities in total)
• 機能のキーワード: pas, lov, gaf, domains fold, signaling protein
• 由来する生物種: Halorhodospira halophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14052.73

構造登録者

Getzoff, E.D.,Gutwin, K.N.,Genick, U.K. (登録日: 2003-02-07, 公開日: 2003-03-11, 最終更新日: 2025-03-26)

主引用文献

Getzoff, E.D.,Gutwin, K.N.,Genick, U.K.
Anticipatory active-site motions and chromophore distortions prime photoreceptor PYP for light activation
Nat.Struct.Biol., 10:663-668, 2003

PubMed Abstract: Protein photoreceptors use small-molecule cofactors called chromophores to detect light. Only under the influence of the receptors' active sites do these chromophores adopt spectral and photochemical properties that suit the receptors' functional requirements. This protein-induced change in chromophore properties is called photochemical tuning and is a prime example for the general--but poorly understood--process of chemical tuning through which proteins shape the reactivity of their active-site groups. Here we report the 0.82-A resolution X-ray structure of the bacterial light receptor photoactive yellow protein (PYP). The unusually precise structure reveals deviations from expected molecular geometries and anisotropic atomic displacements in the PYP active site. Our analysis of these deviations points directly to the intramolecular forces and active-site dynamics that tune the properties of PYP's chromophore to absorb blue light, suppress fluorescence, and favor the required light-driven double-bond isomerization.

PubMed: 12872160
DOI: 10.1038/nsb958

実験手法

X-RAY DIFFRACTION (0.82 Å)