2HFO

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

Summary for 2HFO

• Entry DOI: 10.2210/pdb2hfo/pdb
• Related: 2HFN
• Descriptor: Activator of photopigment and puc expression, FLAVIN MONONUCLEOTIDE (3 entities in total)
• Functional Keywords: beta sheet ferredoxin-like fold, flavin binding protein, photoreceptor, electron transport
• Biological source: Synechocystis sp.
• Total number of polymer chains: 10
• Total formula weight: 180803.62

Authors

Yuan, H.,Anderson, S.,Masuda, S.,Dragnea, V.,Moffat, K.,Bauer, C.E. (deposition date: 2006-06-24, release date: 2006-12-19, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)