2WHS

Fluorescent Protein mKeima at pH 3.8

Summary for 2WHS

Entry DOI	10.2210/pdb2whs/pdb
Related	2WHT 2WHU
Descriptor	LARGE STOKES SHIFT FLUORESCENT PROTEIN, SULFATE ION (3 entities in total)
Functional Keywords	fluorescent protein, stokes shift, mkeima
Biological source	Montipora sp. 20
Total number of polymer chains	4
Total formula weight	109983.44
Authors	Violot, S.,Carpentier, P.,Blanchoin, L.,Bourgeois, D. (deposition date: 2009-05-06, release date: 2009-08-11, Last modification date: 2024-11-13)
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: 19722611 DOI: 10.1021/JA903695N PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.1 Å)

Structure validation