First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.
|3dqc, resolution 1.49Å ()|
|Gene:||GFP (Aequorea victoria)|
|Related:||1huy, 1yfp, 2yfp, 1f0b, 1f09, 3dpw, 3dpx, 3dpz, 3dq1, 3dq2, 3dq3, 3dq4, 3dq5, 3dq6, 3dq7, 3dq8, 3dq9, 3dqa, 3dqd, 3dqe, 3dqf, 3dqh, 3dqi, 3dqj, 3dqk, 3dql, 3dqm, 3dqn, 3dqo, 3dqu|
Structure of the Yellow Fluorescent Protein Citrine Frozen at 1250 Atmospheres Number 3: Structure 13 in a Series of 26 High Pressure Structures
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.
Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift., Barstow B, Ando N, Kim CU, Gruner SM, Proc Natl Acad Sci U S A. 2008 Sep 9;105(36):13362-6. Epub 2008 Sep 3. PMID:18768811
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Alyssa Marsico/Sandbox 1
- Devon McCarthy/Sandbox 1
- Green Fluorescent Protein
- User:Joanne Lau/Sandbox 5
- Barstow B, Ando N, Kim CU, Gruner SM. Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift. Proc Natl Acad Sci U S A. 2008 Sep 9;105(36):13362-6. Epub 2008 Sep 3. PMID:18768811
- Kim CU, Kapfer R, Gruner SM. High-pressure cooling of protein crystals without cryoprotectants. Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):881-90. Epub 2005, Jun 24. PMID:15983410 doi:10.1107/S090744490500836X