1MZU

Crystal Structure of the Photoactive Yellow Protein Domain from the Sensor Histidine Kinase Ppr from Rhodospirillum centenum

1MZU の概要

• エントリーDOI: 10.2210/pdb1mzu/pdb
• 関連するPDBエントリー: 1G28 1GSV 2PHY 2PYP
• 分子名称: PPR, 4'-HYDROXYCINNAMIC ACID (3 entities in total)
• 機能のキーワード: photoactive yellow protein, pas, pyp, ppr, signaling protein
• 由来する生物種: Rhodospirillum centenum
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 44035.63

構造登録者

Rajagopal, S.,Moffat, K. (登録日: 2002-10-09, 公開日: 2003-02-25, 最終更新日: 2025-03-26)

主引用文献

Rajagopal, S.,Moffat, K.
Crystal Structure of a Photoactive Yellow Protein from a Sensor Histidine Kinase: Conformational Variability and Signal Transduction
Proc.Natl.Acad.Sci.USA, 100:1649-1654, 2003

PubMed Abstract: Photoactive yellow protein (E-PYP) is a blue light photoreceptor, implicated in a negative phototactic response in Ectothiorhodospira halophila, that also serves as a model for the Per-Arnt-Sim superfamily of signaling molecules. Because no biological signaling partner for E-PYP has been identified, it has not been possible to correlate any of its photocycle intermediates with a relevant signaling state. However, the PYP domain (Ppr-PYP) from the sensor histidine kinase Ppr in Rhodospirillum centenum, which regulates the catalytic activity of Ppr by blue light absorption, may allow such issues to be addressed. Here we report the crystal structure of Ppr-PYP at 2 A resolution. This domain has the same absorption spectrum and similar photocycle kinetics as full length Ppr, but a blue-shifted absorbance and considerably slower photocycle than E-PYP. Although the overall fold of Ppr-PYP resembles that of E-PYP, a novel conformation of the beta 4-beta 5 loop results in inaccessibility of Met-100, thought to catalyze chromophore reisomerization, to the chromophore. This conformation also exposes a highly conserved molecular surface that could interact with downstream signaling partners. Other structural differences in the alpha 3-alpha 4 and beta 4-beta 5 loops are consistent with these regions playing significant roles in the control of photocycle dynamics and, by comparison to other sensory Per-Arnt-Sim domains, in signal transduction. Because of its direct linkage to a measurable biological output, Ppr-PYP serves as an excellent system for understanding how changes in photocycle dynamics affect signaling by PYPs.

PubMed: 12563032
DOI: 10.1073/pnas.0336353100

実験手法

X-RAY DIFFRACTION (2 Å)