1XQM

Variations on the GFP chromophore scaffold: A fragmented 5-membered heterocycle revealed in the 2.1A crystal structure of a non-fluorescent chromoprotein

Summary for 1XQM

• Entry DOI: 10.2210/pdb1xqm/pdb
• Descriptor: kindling fluorescent protein, ACETIC ACID (3 entities in total)
• Functional Keywords: luminescent protein
• Total number of polymer chains: 1
• Total formula weight: 25898.54

Authors

Wilmann, P.G.,Petersen, J.,Devenish, R.J.,Prescott, M.,Rossjohn, J. (deposition date: 2004-10-13, release date: 2004-11-16, Last modification date: 2024-10-09)

Primary citation

Wilmann, P.G.,Petersen, J.,Devenish, R.J.,Prescott, M.,Rossjohn, J.
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
J.Biol.Chem., 280:2401-2404, 2005

PubMed Abstract: 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.

PubMed: 15542608
DOI: 10.1074/jbc.C400484200

Experimental method

X-RAY DIFFRACTION (2.1 Å)