2FL1

Crystal structure of red fluorescent protein from Zoanthus, zRFP574, at 2.4A resolution

Summary for 2FL1

• Entry DOI: 10.2210/pdb2fl1/pdb
• Related: 1XA9
• Descriptor: Red fluorescent protein zoanRFP, SULFATE ION (3 entities in total)
• Functional Keywords: red fluorescent protein, button polyp, zoanthus sp., chromophore, beta-can fold, beta barrel, tightly packed tetramer, intersubunit interface, fluorescent marker, emission maximum 574nm, zrfp574, fluorescent protein
• Biological source: Zoanthus sp.
• Total number of polymer chains: 4
• Total formula weight: 104770.51

Authors

Pletnev, V.,Pletneva, N.,Martynov, V.,Tikhonova, T.,Popov, B.,Pletnev, S. (deposition date: 2006-01-05, release date: 2007-01-09, Last modification date: 2024-11-20)

Primary citation

Pletneva, N.,Pletnev, S.,Tikhonova, T.,Popov, V.,Martynov, V.,Pletnev, V.
Structure of a red fluorescent protein from Zoanthus, zRFP574, reveals a novel chromophore
Acta Crystallogr.,Sect.D, 62:527-532, 2006

PubMed Abstract: The three-dimensional structure of the red fluorescent protein (RFP) zRFP574 from the button polyp Zoanthus sp. (two dimers per asymmetric unit, 231 x 4 amino acids) has been determined at 2.4 A resolution in space group C222(1). The crystal structure, refined to a crystallographic R factor of 0.203 (R(free) = 0.249), adopts the beta-barrel fold composed of 11 strands similar to that of the yellow fluorescent protein zYFP538. The zRFP574 chromophore, originating from the protein sequence Asp66-Tyr67-Gly68, has a two-ring structure typical of GFP-like proteins. The bond geometry of residue 66 shows the strong tendency of the corresponding C(alpha) atom to sp(2) hybridization as a consequence of N-acylimine bond formation. The zRFP574 chromophore contains the 65-66 cis-peptide bond characteristic of red fluorescent proteins. The chromophore phenolic ring adopts a cis conformation coplanar with the imidazolinone ring. The crystallographic study has revealed an unexpected chemical feature of the internal chromophore. A decarboxylated side chain of the chromophore-forming residue Asp66 has been observed in the structure. This additional post-translational modification is likely to play a key role in the bathochromic shift of the zRFP574 spectrum.

PubMed: 16627946
DOI: 10.1107/S0907444906007852

Experimental method

X-RAY DIFFRACTION (2.4 Å)