PDBsum entry 5dkl

Signaling protein

PDB id: 5dkl

Contents

Protein chains

133 a.a.

Ligands

FMN ×2

Waters ×2

PDB id:

5dkl

Name:

Signaling protein

Title:

Structure of the light-state dimer of the blue light photoreceptor aureochrome 1a lov from p. Tricornutum

Structure:

Lov domain. Chain: a, b. Fragment: unp residues 234-378. Engineered: yes

Source:

Phaeodactylum tricornutum. Organism_taxid: 2850. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.70Å R-factor: 0.211 R-free: 0.243

Authors:

U.Heintz,I.Schlichting

Key ref:

U.Heintz and I.Schlichting (2016). Blue light-induced LOV domain dimerization enhances the affinity of Aureochrome 1a for its target DNA sequence. Elife, 5, e11860. PubMed id: 26754770 DOI: 10.7554/eLife.11860

Date:

03-Sep-15 Release date: 13-Jan-16

Protein chains

B7G9J2  (B7G9J2_PHATC) -  LOV domain-containing protein (Fragment) from Phaeodactylum tricornutum (strain CCAP 1055/1)

Seq: 103 a.a.

Struc: 133 a.a.

DOI no: 10.7554/eLife.11860

Elife 5:e11860 (2016)

PubMed id: 26754770

Blue light-induced LOV domain dimerization enhances the affinity of Aureochrome 1a for its target DNA sequence.

U.Heintz, I.Schlichting.

ABSTRACT

The design of synthetic optogenetic tools that allow precise spatiotemporal control of biological processes previously inaccessible to optogenetic control has developed rapidly over the last years. Rational design of such tools requires detailed knowledge of allosteric light signaling in natural photoreceptors. To understand allosteric communication between sensor and effector domains, characterization of all relevant signaling states is required. Here, we describe the mechanism of light-dependent DNA binding of the light-oxygen-voltage (LOV) transcription factor Aureochrome 1a from Phaeodactylum tricornutum (PtAu1a) and present crystal structures of a dark state LOV monomer and a fully light-adapted LOV dimer. In combination with hydrogen/deuterium-exchange, solution scattering data and DNA-binding experiments, our studies reveal a light-sensitive interaction between the LOV and basic region leucine zipper DNA-binding domain that together with LOV dimerization results in modulation of the DNA affinity of PtAu1a. We discuss the implications of these results for the design of synthetic LOV-based photosensors with application in optogenetics.