4HNB

Crystal Structure of Rhodobacter Sphaeroides LOV protein

Summary for 4HNB

• Entry DOI: 10.2210/pdb4hnb/pdb
• Related: 4HIA 4HJ3 4HJ4 4HJ6
• Descriptor: LOV protein, FLAVIN MONONUCLEOTIDE, 1-DEOXY-1-(7,8-DIMETHYL-2,4-DIOXO-3,4-DIHYDRO-2H-BENZO[G]PTERIDIN-1-ID-10(5H)-YL)-5-O-PHOSPHONATO-D-RIBITOL, ... (4 entities in total)
• Functional Keywords: lov pas hth, signaling, signaling protein
• Biological source: Rhodobacter sphaeroides
• Total number of polymer chains: 2
• Total formula weight: 39976.86

Authors

Crane, B.R.,Conrad, K.S.,Bilwes, A.M. (deposition date: 2012-10-19, release date: 2013-01-16, Last modification date: 2024-03-13)

Primary citation

Conrad, K.S.,Bilwes, A.M.,Crane, B.R.
Light-induced subunit dissociation by a light-oxygen-voltage domain photoreceptor from Rhodobacter sphaeroides.
Biochemistry, 52:378-391, 2013

PubMed Abstract: Light-oxygen-voltage (LOV) domains bind a flavin chromophore to serve as blue light sensors in a wide range of eukaryotic and prokaryotic proteins. LOV domains are associated with a variable effector domain or a separate protein signaling partner to execute a wide variety of functions that include regulation of kinases, generation of anti-sigma factor antagonists, and regulation of circadian clocks. Here we present the crystal structure, photocycle kinetics, association properties, and spectroscopic features of a full-length LOV domain protein from Rhodobacter sphaeroides (RsLOV). RsLOV exhibits N- and C-terminal helical extensions that form an unusual helical bundle at its dimer interface with some resemblance to the helical transducer of sensory rhodopsin II. The blue light-induced conformational changes of RsLOV revealed from a comparison of light- and dark-state crystal structures support a shared signaling mechanism of LOV domain proteins that originates with the light-induced formation of a flavin-cysteinyl photoadduct. Adduct formation disrupts hydrogen bonding in the active site and propagates structural changes through the LOV domain core to the N- and C-terminal extensions. Single-residue variants in the active site and dimer interface of RsLOV alter photoadduct lifetimes and induce structural changes that perturb the oligomeric state. Size exclusion chromatography, multiangle light scattering, small-angle X-ray scattering, and cross-linking studies indicate that RsLOV dimerizes in the dark but, upon light excitation, dissociates into monomers. This light-induced switch in oligomeric state may prove to be useful for engineering molecular associations in controlled cellular settings.

PubMed: 23252338
DOI: 10.1021/bi3015373

Experimental method

X-RAY DIFFRACTION (2.34 Å)