1xqm
From Proteopedia
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Variations on the GFP chromophore scaffold: A fragmented 5-membered heterocycle revealed in the 2.1A crystal structure of a non-fluorescent chromoprotein
Overview
We have determined to 2.1 A resolution the crystal structure of a dark, state, kindling fluorescent protein isolated from the sea anemone, Anemonia sulcata. The chromophore sequence Met(63)-Tyr(64)-Gly(65) of the, A. sulcata chromoprotein was previously proposed to comprise a 6-membered, pyrazine-type heterocycle (Martynov, V. I., Savitsky, A. P., Martynova, N., Y., Savitsky, P. A., Lukyanov, K. A., and Lukyanov, S. A. (2001) J. Biol., Chem. 276, 21012-21016). However, our crystallographic data revealed the, chromophore to comprise a 5-membered p-hydroxybenzylideneimidazolinone, moiety that adopts a non-coplanar trans conformation within the interior, of the GFP beta-can fold. Unexpectedly, fragmentation of the polypeptide, was found to occur within the chromophore moiety, at the bond between, Cys(62C) and Met(63N1.) Our structural data reveal that fragmentation of, the chromophore represents an intrinsic, autocatalytic step toward the, formation of the mature chromophore within the specific GFP-like proteins.
About this Structure
1XQM is a Single protein structure of sequence from [1] with ACY as ligand. Full crystallographic information is available from OCA.
Reference
Variations on the GFP chromophore: A polypeptide fragmentation within the chromophore revealed in the 2.1-A crystal structure of a nonfluorescent chromoprotein from Anemonia sulcata., Wilmann PG, Petersen J, Devenish RJ, Prescott M, Rossjohn J, J Biol Chem. 2005 Jan 28;280(4):2401-4. Epub 2004 Nov 12. PMID:15542608
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