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J. Biol. Chem., Vol. 278, Issue 45, 44626-44631, November 7, 2003

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The 2.0-Å Crystal Structure of eqFP611, a Far Red Fluorescent Protein from the Sea Anemone Entacmaea quadricolor^*

From the ^aThe Protein Crystallography Unit and the ^bDepartment of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton Campus, Victoria 3800, Australia, and the ^fDepartment of Pharmacology/Crystallography Centre, University of Western Australia, Crawley, Western Australia 6009, Australia

We have crystallized and subsequently determined to 2.0-Å resolution the crystal structure of eqFP611, a far red fluorescent protein from the sea anemone Entacmaea quadricolor. The structure of the protomer, which adopts a -can topology, is similar to that of the related monomeric green fluorescent protein (GFP). The quaternary structure of eqFP611, a tetramer exhibiting 222 symmetry, is similar to that observed for the more closely related red fluorescent protein DsRed and the chromoprotein Rtms5. The unique chromophore sequence (Met⁶³-Tyr⁶⁴-Gly⁶⁵) of eqFP611, adopts a coplanar and trans conformation within the interior of the -can fold. Accordingly, the eqFP611 chromophore adopts a significantly different conformation in comparison to the chromophore conformation observed in GFP, DsRed, and Rtms5. The coplanar chromophore conformation and its immediate environment provide a structural basis for the far red, highly fluorescent nature of eqFP611. The eqFP611 structure extends our knowledge on the range of conformations a chromophore can adopt within closely related members of the green fluorescent protein family.

Received for publication, July 21, 2003 , and in revised form, August 8, 2003.

The atomic coordinates and structure factors (code 1UIS) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by the Australian Research Council and a Monash University small grant. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^c Both authors contributed equally to this work.

^d Supported by the Landesgraduiertenförderung of Baden-Württemberg, the German Academic Exchange Service DAAD and Prof. P. Gräber.

^e Supported by a Monash University Ph.D. scholarship.

^g Supported by an Australian Research Council Postdoctoral Fellowship.

^h To whom correspondence may be addressed. Tel.: 61-3-9905-3724; Fax: 61-3-9905-3726; E-mail: Mark.Prescott{at}med.monash.edu.au.

ⁱ Supported by a Wellcome Trust Senior Research Fellowship in Biomedical Science in Australia. To whom correspondence may be addressed. Tel.: 61-3-9905-3736; Fax: 61-3-9905-3726; E-mail: Jamie.rossjohn{at}med.monash.edu.au.

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