PDBsum entry 3dq7

Luminescent protein

PDB id: 3dq7

Contents

Protein chain

231 a.a. *

Waters ×273

* Residue conservation analysis

PDB id:

3dq7

Name:

Luminescent protein

Title:

Structure of the yellow fluorescent protein citrine frozen at 1920 atmospheres number 1: structure 17 in a series of 26 high pressure structures

Structure:

Green fluorescent protein. Chain: a. Engineered: yes. Mutation: yes

Source:

Aequorea victoria. Jellyfish. Organism_taxid: 6100. Gene: gfp. Expressed in: escherichia coli.

Resolution:

1.23Å R-factor: 0.212 R-free: 0.250

Authors:

B.Barstow,C.U.Kim

Key ref:

B.Barstow et al. (2008). Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift. Proc Natl Acad Sci U S A, 105, 13362-13366. PubMed id: 18768811 DOI: 10.1073/pnas.0802252105

Date:

09-Jul-08 Release date: 23-Sep-08

Protein chain

P42212  (GFP_AEQVI) -  Green fluorescent protein from Aequorea victoria

Seq: 238 a.a.

Struc: 231 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

DOI no: 10.1073/pnas.0802252105

Proc Natl Acad Sci U S A 105:13362-13366 (2008)

PubMed id: 18768811

Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift.

B.Barstow, N.Ando, C.U.Kim, S.M.Gruner.

ABSTRACT

A protein molecule is an intricate system whose function is highly sensitive to small external perturbations. However, no examples that correlate protein function with progressive subangstrom structural perturbations have thus far been presented. To elucidate this relationship, we have investigated a fluorescent protein, citrine, as a model system under high-pressure perturbation. The protein has been compressed to produce deformations of its chromophore by applying a high-pressure cryocooling technique. A closely spaced series of x-ray crystallographic structures reveals that the chromophore undergoes a progressive deformation of up to 0.8 A at an applied pressure of 500 MPa. It is experimentally demonstrated that the structural motion is directly correlated with the progressive fluorescence shift of citrine from yellow to green under these conditions. This protein is therefore highly sensitive to subangstrom deformations and its function must be understood at the subangstrom level. These results have significant implications for protein function prediction and biomolecule design and engineering, because they suggest methods to tune protein function by modification of the protein scaffold.

Selected figure(s)

Figure 1.
The citrine molecule and citrine's chromophore.

Figure 4.
Average center of mass positions of the main chromophore phenol and imidazolinone rings in the coordinate system defined in Fig. 3. Error bars were estimated by Cruickshank's formula. Fits are shown as solid gray lines.

Figures were selected by an automated process.