2whs

Fluorescent Protein mKeima at pH 3.8

spinqualitylabelsall models 2whs, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2whs 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 2.1Å Ligands: CRQ, SO4 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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