2PYP

PHOTOACTIVE YELLOW PROTEIN, PHOTOSTATIONARY STATE, 50% GROUND STATE, 50% BLEACHED

2PYP の概要

• エントリーDOI: 10.2210/pdb2pyp/pdb
• 分子名称: Photoactive yellow protein (2 entities in total)
• 機能のキーワード: photoreceptor, chromophore, light sensor for phototaxis
• 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: 14034.72

構造登録者

Genick, U.K.,Borgstahl, G.E.O.,Ng, K.,Ren, Z.,Pradervand, C.,Burke, P.,Srajer, V.,Teng, T.,Schildkamp, W.,Mcree, D.E.,Moffat, K.,Getzoff, E.D. (登録日: 1997-02-03, 公開日: 1998-04-29, 最終更新日: 2024-12-25)

主引用文献

Genick, U.K.,Borgstahl, G.E.,Ng, K.,Ren, Z.,Pradervand, C.,Burke, P.M.,Srajer, V.,Teng, T.Y.,Schildkamp, W.,McRee, D.E.,Moffat, K.,Getzoff, E.D.
Structure of a protein photocycle intermediate by millisecond time-resolved crystallography.
Science, 275:1471-1475, 1997

PubMed Abstract: The blue-light photoreceptor photoactive yellow protein (PYP) undergoes a self-contained light cycle. The atomic structure of the bleached signaling intermediate in the light cycle of PYP was determined by millisecond time-resolved, multiwavelength Laue crystallography and simultaneous optical spectroscopy. Light-induced trans-to-cis isomerization of the 4-hydroxycinnamyl chromophore and coupled protein rearrangements produce a new set of active-site hydrogen bonds. An arginine gateway opens, allowing solvent exposure and protonation of the chromophore's phenolic oxygen. Resulting changes in shape, hydrogen bonding, and electrostatic potential at the protein surface form a likely basis for signal transduction. The structural results suggest a general framework for the interpretation of protein photocycles.

PubMed: 9045611
DOI: 10.1126/science.275.5305.1471

実験手法

X-RAY DIFFRACTION (1.9 Å)