title: Crystal structures of the Synechocystis photoreceptor Slr1694 reveal distinct structural states related to signaling.
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.
authors.affiliation: Department of Biology, Indiana University, Bloomington, Indiana 47405, USA.
authors.forename: Hua
authors.initials: H
authors.lastname: Yuan
authors.forename: Spencer
authors.initials: S
authors.lastname: Anderson
authors.forename: Shinji
authors.initials: S
authors.lastname: Masuda
authors.forename: Vladimira
authors.initials: V
authors.lastname: Dragnea
authors.forename: Keith
authors.initials: K
authors.lastname: Moffat
authors.forename: Carl
authors.initials: C
authors.lastname: Bauer
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D046939:Synechocystis / Q000737:chemistry*; D014364:Tryptophan
chemical_list: D001426:Bacterial Proteins; D014364:Tryptophan