2wht

Fluorescent Protein mKeima at pH 5.6Fluorescent Protein mKeima at pH 5.6

Structural highlights

2wht is a 4 chain structure with sequence from Montipora sp. 20. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q1JV70_9CNID

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Reverse pH-dependence of chromophore protonation explains the large Stokes shift of the red fluorescent protein mKeima.,Violot S, Carpentier P, Blanchoin L, Bourgeois D J Am Chem Soc. 2009 Aug 5;131(30):10356-7. PMID:19722611^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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. 2009 Aug 5;131(30):10356-7. PMID:19722611 doi:10.1021/ja903695n

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OCA

[1] 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. 2009 Aug 5;131(30):10356-7. PMID:19722611 doi:10.1021/ja903695n

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