PDBsum entry 2v0u

Transferase

PDB id: 2v0u

Contents

Protein chain

146 a.a. *

Ligands

FMN

GOL ×6

Waters ×173

* Residue conservation analysis

PDB id:

2v0u

Name:

Transferase

Title:

N- and c-terminal helices of oat lov2 (404-546) are involved in light- induced signal transduction (cryo dark structure of lov2 (404-546))

Structure:

Nph1-1. Chain: a. Fragment: light, oxygen, voltage domain, residues 404-546. Synonym: lov2. Engineered: yes

Source:

Avena sativa. Oat. Organism_taxid: 4498. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.40Å R-factor: 0.167 R-free: 0.197

Authors:

A.S.Halavaty,K.Moffat

Key ref:

A.S.Halavaty and K.Moffat (2007). N- and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa. Biochemistry, 46, 14001-14009. PubMed id: 18001137

Date:

18-May-07 Release date: 11-Dec-07

Protein chain

O49003  (O49003_AVESA) -  non-specific serine/threonine protein kinase from Avena sativa

Seq: 923 a.a.

Struc: 146 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.2.7.11.1 - non-specific serine/threonine protein kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

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

reference

Biochemistry 46:14001-14009 (2007)

PubMed id: 18001137

N- and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa.

A.S.Halavaty, K.Moffat.

ABSTRACT

Light sensing by photoreceptors controls phototropism, chloroplast movement, stomatal opening, and leaf expansion in plants. Understanding the molecular mechanism by which these processes are regulated requires a quantitative description of photoreceptor dynamics. We focus on a light-driven signal transduction mechanism in the LOV2 domain (LOV, light, oxygen, voltage) of the blue light photoreceptor phototropin 1 from Avena sativa (oat). High-resolution crystal structures of the dark and light states of an oat LOV2 construct including residues Leu404 through Leu546 (LOV2 (404-546)) have been determined at 105 and 293 K. In all four structures, LOV2 (404-546) exhibits the typical Per-ARNT-Sim (PAS) fold, flanked by an additional conserved N-terminal turn-helix-turn motif and a C-terminal flanking region containing an amphipathic Jalpha helix. These regions dock on the LOV2 core domain and bury several hydrophobic residues of the central beta-sheet of the core domain that would otherwise be exposed to solvent. Light structures of LOV2 (404-546) reveal that formation of the covalent bond between Cys450 and the C4a atom of the flavin mononucleotide (FMN) results in local rearrangement of the hydrogen-bonding network in the FMN binding pocket. These rearrangements are associated with disruption of the Asn414-Asp515 hydrogen bond on the surface of the protein and displacement of the N- and C-terminal flanking regions of LOV2 (404-546), both of which constitute a structural signal.