1UIS

The 2.0 crystal structure of eqFP611, a far-red fluorescent protein from the sea anemone Entacmaea quadricolor

Summary for 1UIS

• Entry DOI: 10.2210/pdb1uis/pdb
• Related: 1GGX 1MOU 1MOV
• Descriptor: red fluorescent protein FP611, CALCIUM ION, ACETIC ACID, ... (4 entities in total)
• Functional Keywords: luminescent protein
• Biological source: Entacmaea quadricolor
• Total number of polymer chains: 2
• Total formula weight: 52828.37

Authors

Petersen, J.,Wilmann, P.G.,Beddoe, T.,Oakley, A.J.,Devenish, R.J.,Prescott, M.,Rossjohn, J. (deposition date: 2003-07-21, release date: 2003-10-21, Last modification date: 2023-12-27)

Primary citation

Petersen, J.,Wilmann, P.G.,Beddoe, T.,Oakley, A.J.,Devenish, R.J.,Prescott, M.,Rossjohn, J.
The 2.0A crystal structure of eqFP611, a far-red fluorescent protein from the sea anemone Entacmaea quadricolor
J.Biol.Chem., 278:44626-44631, 2003

PubMed Abstract: We have crystallized and subsequently determined to 2.0-A 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 beta-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 beta-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.

PubMed: 12909624
DOI: 10.1074/jbc.M307896200

Experimental method

X-RAY DIFFRACTION (2 Å)