PDBsum entry 4gcz

Signaling protein, de novo protein

PDB id: 4gcz

Contents

Protein chains

366 a.a.

Ligands

FMN ×2

ADP

SO4 ×10

Waters ×451

PDB id:

4gcz

Name:

Signaling protein, de novo protein

Title:

Structure of a blue-light photoreceptor

Structure:

Blue-light photoreceptor, sensor protein fixl. Chain: a, b. Fragment: unp o34627 residues 1-126, unp p23222 residues 257-505. Synonym: photoactive flavo-yellow protein, phototropin homolog. Engineered: yes

Source:

Bacillus subtilis, bradyrhizobium japonicum. Organism_taxid: 224308, 224911. Strain: 168, usda 110. Gene: pfyp, ytva, bsu30340, fixl, bll2760. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.30Å R-factor: 0.181 R-free: 0.217

Authors:

R.P.Diensthuber,M.Bommer,A.Moglich

Key ref:

R.P.Diensthuber et al. (2013). Full-length structure of a sensor histidine kinase pinpoints coaxial coiled coils as signal transducers and modulators. Structure, 21, 1127-1136. PubMed id: 23746806 DOI: 10.1016/j.str.2013.04.024

Date:

31-Jul-12 Release date: 19-Jun-13

Protein chains

O34627  (PHOT_BACSU) -  Blue-light photoreceptor from Bacillus subtilis (strain 168)

Seq: 261 a.a.

Struc: 366 a.a.*

Protein chains

P23222  (FIXL_BRADU) -  Sensor protein FixL from Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)

Seq: 505 a.a.

Struc: 366 a.a.*

* PDB and UniProt seqs differ at 205 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.2.7.13.3 - histidine kinase.
• Reaction: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine

ATP + protein L-histidine = ADP (Bound ligand (Het Group name = ADP) corresponds exactly) + protein N-phospho-L-histidine

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.str.2013.04.024

Structure 21:1127-1136 (2013)

PubMed id: 23746806

Full-length structure of a sensor histidine kinase pinpoints coaxial coiled coils as signal transducers and modulators.

R.P.Diensthuber, M.Bommer, T.Gleichmann, A.Möglich.

ABSTRACT

Two-component systems (TCSs), which comprise sensor histidine kinases (SHK) and response-regulator proteins, represent the predominant strategy by which prokaryotes sense and respond to a changing environment. Despite paramount biological importance, a dearth exists of intact SHK structures containing both sensor and effector modules. Here, we report the full-length crystal structure of the engineered, dimeric, blue-light-regulated SHK YF1 at 2.3 Å resolution, in which two N-terminal light-oxygen-voltage (LOV) photosensors are connected by a coiled coil to the C-terminal effector modules. A second coaxial coiled coil derived from the N-termini of the LOV photosensors and inserted between them crucially modulates light regulation: single mutations within this coiled coil attenuate or even invert the signal response of the TCS. Structural motifs identified in YF1 recur in signal receptors, and the underlying signaling principles and mechanisms may be widely shared between soluble and transmembrane, prokaryotic, and eukaryotic signal receptors of diverse biological activity.