2WHU
Fluorescent Protein mKeima at pH 8.0
Summary for 2WHU
Entry DOI | 10.2210/pdb2whu/pdb |
Related | 2WHS 2WHT |
Descriptor | LARGE STOKES SHIFT FLUORESCENT PROTEIN (2 entities in total) |
Functional Keywords | mkeima, stokes shift, fluorescent protein |
Biological source | Montipora sp. 20 |
Total number of polymer chains | 4 |
Total formula weight | 108926.74 |
Authors | Violot, S.,Carpentier, P.,Blanchoin, L.,Bourgeois, D. (deposition date: 2009-05-06, release date: 2009-08-11, Last modification date: 2024-10-23) |
Primary citation | Violot, S.,Carpentier, P.,Blanchoin, L.,Bourgeois, D. Reverse Ph-Dependence of Chromophore Protonation Explains the Large Stokes Shift of the Red Fluorescent Protein Mkeima J.Am.Chem.Soc., 131:10356-, 2009 Cited by PubMed Abstract: The recently developed red fluorescent protein Keima exhibits the largest Stokes shift (180 nm) observed to date. Combining X-ray crystallography with (in crystallo) UV-visible absorption, fluorescence, and Raman spectroscopy, we have investigated molecular determinants of this peculiar property. The results demonstrate a pH-dependent "reverse chromophore protonation" triggered by the key residue Asp157 and which couples to cis/trans isomerization of the chromophore. These data provided guidelines to rationally design a useful Keima variant. PubMed: 19722611DOI: 10.1021/JA903695N PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
Download full validation report