2HFO

Crystal Structures of the Synechocystis Photoreceptor Slr1694 Reveal Distinct Structural States Related to Signaling

2HFO の概要

• エントリーDOI: 10.2210/pdb2hfo/pdb
• 関連するPDBエントリー: 2HFN
• 分子名称: Activator of photopigment and puc expression, FLAVIN MONONUCLEOTIDE (3 entities in total)
• 機能のキーワード: beta sheet ferredoxin-like fold, flavin binding protein, photoreceptor, electron transport
• 由来する生物種: Synechocystis sp.
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 180803.62

構造登録者

Yuan, H.,Anderson, S.,Masuda, S.,Dragnea, V.,Moffat, K.,Bauer, C.E. (登録日: 2006-06-24, 公開日: 2006-12-19, 最終更新日: 2024-02-14)

主引用文献

Yuan, H.,Anderson, S.,Masuda, S.,Dragnea, V.,Moffat, K.,Bauer, C.E.
Crystal structures of the Synechocystis photoreceptor Slr1694 reveal distinct structural states related to signaling.
Biochemistry, 45:12687-12694, 2006

PubMed Abstract: Crystal structures of the Synechocystis BLUF phototaxis photoreceptor Slr1694 have been determined in two crystal forms, a monoclinic form at 1.8 A resolution and an orthorhombic form at 2.1 A resolution. In both forms, the photoreceptor is comprised of two pentamer rings stacked face to face. Twenty total subunits in the two asymmetric units of these crystal forms display three distinct tertiary structures that differ in the length of the fifth beta-strand and in the orientation of Trp91, a conserved Trp residue near the FMN chromophore. Fluorescence spectroscopic analysis on Slr1694 in solution is consistent with motion of Trp91 from a hydrophobic environment in the dark state to a more hydrophilic environment in the light-excited state. Mutational analysis indicates that movement of Trp91 is dependent on the occupancy of the hydrophobic Trp binding pocket with a nearby Met. These different tertiary structures may be associated with absorption changes in the blue region of the spectrum.

PubMed: 17042486
DOI: 10.1021/bi061435n

実験手法

X-RAY DIFFRACTION (2.1 Å)