PDBsum entry 5j4e

Signaling protein

PDB id: 5j4e

Contents

Protein chains

133 a.a.

Ligands

FMN ×4

PDB id:

5j4e

Name:

Signaling protein

Title:

Crystal structures reveal signaling states of a short blue light photoreceptor protein ppsb1-lov (photoexcited state)

Structure:

Sensory box protein. Chain: a, b, c, d. Synonym: lov protein. Engineered: yes

Source:

Pseudomonas putida. Organism_taxid: 303. Gene: pp_4629. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.67Å R-factor: 0.190 R-free: 0.261

Authors:

J.Granzin,R.Batra-Safferling

Key ref:

K.Röllen et al. (2016). Signaling States of a Short Blue-Light Photoreceptor Protein PpSB1-LOV Revealed from Crystal Structures and Solution NMR Spectroscopy. J Mol Biol, 428, 3721-3736. PubMed id: 27291287 DOI: 10.1016/j.jmb.2016.05.027

Date:

01-Apr-16 Release date: 22-Jun-16

Protein chains

Q88E39  (Q88E39_PSEPK) -  Sensory box protein from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

Seq: 142 a.a.

Struc: 133 a.a.

DOI no: 10.1016/j.jmb.2016.05.027

J Mol Biol 428:3721-3736 (2016)

PubMed id: 27291287

Signaling States of a Short Blue-Light Photoreceptor Protein PpSB1-LOV Revealed from Crystal Structures and Solution NMR Spectroscopy.

K.Röllen, J.Granzin, V.Panwalkar, V.Arinkin, R.Rani, R.Hartmann, U.Krauss, K.E.Jaeger, D.Willbold, R.Batra-Safferling.

ABSTRACT

Light-Oxygen-Voltage (LOV) domains represent the photo-responsive domains of various blue-light photoreceptor proteins and are widely distributed in plants, algae, fungi, and bacteria. Here, we report the dark-state crystal structure of PpSB1-LOV, a slow-reverting short LOV protein from Pseudomonas putida that is remarkably different from our previously published "fully light-adapted" structure [1]. A direct comparison of the two structures provides insight into the light-activated signaling mechanism. Major structural differences involve a~11Å movement of the C terminus in helix Jα, ~4Å movement of Hβ-Iβ loop, disruption of hydrogen bonds in the dimer interface, and a~29° rotation of chain-B relative to chain-A as compared to the light-state dimer. Both crystal structures and solution NMR data are suggestive of the key roles of a conserved glutamine Q116 and the N-cap region consisting of A'α-Aβ loop and the A'α helix in controlling the light-activated conformational changes. The activation mechanism proposed here for the PpSB1-LOV supports a rotary switch mechanism and provides insights into the signal propagation mechanism in naturally existing and artificial LOV-based, two-component systems and regulators.