PDBsum entry 4cqh

Fluorescent protein

PDB id: 4cqh

Contents

Protein chain

306 a.a.

Ligands

LBV

Metals

_NA

Waters ×293

PDB id:

4cqh

Name:

Fluorescent protein

Title:

Structure of infrared fluorescent protein ifp2.0

Structure:

Bacteriophytochrome. Chain: a. Fragment: residues 1-317. Synonym: phytochrome-like protein, infrared fluorescent protein version 2.0. Engineered: yes. Mutation: yes

Source:

Deinococcus radiodurans. Organism_taxid: 1299. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: ril.

Resolution:

1.14Å R-factor: 0.138 R-free: 0.160

Authors:

C.Lafaye,D.Yu,M.Noirclerc-Savoye,X.Shu,A.Royant

Key ref:

D.Yu et al. (2014). An improved monomeric infrared fluorescent protein for neuronal and tumour brain imaging. Nat Commun, 5, 3626. PubMed id: 24832154 DOI: 10.1038/ncomms4626

Date:

17-Feb-14 Release date: 28-May-14

Protein chain

Q9RZA4  (BPHY_DEIRA) -  Bacteriophytochrome from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)

Seq: 755 a.a.

Struc: 306 a.a.*

* PDB and UniProt seqs differ at 13 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

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

reference

DOI no: 10.1038/ncomms4626

Nat Commun 5:3626 (2014)

PubMed id: 24832154

An improved monomeric infrared fluorescent protein for neuronal and tumour brain imaging.

D.Yu, W.C.Gustafson, C.Han, C.Lafaye, M.Noirclerc-Savoye, W.P.Ge, D.A.Thayer, H.Huang, T.B.Kornberg, A.Royant, L.Y.Jan, Y.N.Jan, W.A.Weiss, X.Shu.

ABSTRACT

Infrared fluorescent proteins (IFPs) are ideal for in vivo imaging, and monomeric versions of these proteins can be advantageous as protein tags or for sensor development. In contrast to GFP, which requires only molecular oxygen for chromophore maturation, phytochrome-derived IFPs incorporate biliverdin (BV) as the chromophore. However, BV varies in concentration in different cells and organisms. Here we engineered cells to express the haeme oxygenase responsible for BV biosynthesis and a brighter monomeric IFP mutant (IFP2.0). Together, these tools improve the imaging capabilities of IFP2.0 compared with monomeric IFP1.4 and dimeric iRFP. By targeting IFP2.0 to the plasma membrane, we demonstrate robust labelling of neuronal processes in Drosophila larvae. We also show that this strategy improves the sensitivity when imaging brain tumours in whole mice. Our work shows promise in the application of IFPs for protein labelling and in vivo imaging.