3DPZ
Structure of the Yellow Fluorescent Protein Citrine Frozen at 4000 Atmospheres Number 3: Structure 25 in a Series of 26 High Pressure Structures
Summary for 3DPZ
| Entry DOI | 10.2210/pdb3dpz/pdb |
| Related | 1F09 1F0B 1HUY 1YFP 2YFP 3DPW 3DPX 3DQ1 3DQ2 3DQ3 3DQ4 3DQ5 3DQ6 3DQ7 3DQ8 3DQ9 3DQA 3DQC 3DQD 3DQE 3DQF 3DQH 3DQI 3DQJ 3DQK 3DQL 3DQM 3DQN 3DQO 3DQU |
| Descriptor | Green fluorescent protein (2 entities in total) |
| Functional Keywords | yellow fluorescent protein, beta barrel, chromophore, fluorescent protein, high pressure, luminescence, photoprotein, luminescent protein |
| Biological source | Aequorea victoria (Jellyfish) |
| Total number of polymer chains | 1 |
| Total formula weight | 27393.92 |
| Authors | Barstow, B.,Kim, C.U. (deposition date: 2008-07-09, release date: 2008-09-23, Last modification date: 2024-10-30) |
| Primary citation | Barstow, B.,Ando, N.,Kim, C.U.,Gruner, S.M. Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift. Proc.Natl.Acad.Sci.Usa, 105:13362-13366, 2008 Cited by PubMed 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. PubMed: 18768811DOI: 10.1073/pnas.0802252105 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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