Volume 86 Issue 38 | p. 71 | Concentrates
Issue Date: September 22, 2008

An Unusual Blue Protein Chromophore

Department: Science & Technology
News Channels: JACS In C&EN
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Blue chromophore includes a zinc- coordinated, four-residue cross-linking unit not seen before in a native protein structure.
Credit: Angew. Chem. Int. Ed.

Ranasmurfin, a blue protein isolated from the nests of a type of Malaysian tree frog, has an unusual chromophore, as well as uncommon amino acid cross-links. An international team led by Alan Cooper of the University of Glasgow and James H. Naismith of the University of St. Andrews, both in Scotland, has solved a 1.16-Å crystal structure showing that ranasmurfin, a 26-kilodalton homodimer, is stabilized by unusual lysine tyrosyl quinone (LTQ) linkages (Angew. Chem. Int. Ed., DOI: 10.1002/anie.200802901). This is the first time such modifications have been identified in a native protein. The crystal structure also reveals a four-residue bis(LTQ) linkage between the protein's subunits. The bis(LTQ) structure, together with two histidine residues, serves as the binding site for a Zn2+ ion and is a likely candidate for the protein's blue chromophore. The bridging atom in bis(LTQ) can't be unequivocally identified by just electron density, but the researchers suspect that it's nitrogen because a nitrogen moiety would make a good ligand for zinc, and similar N-linked compounds are often highly colored.

 
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ISSN 0009-2347
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