2C9I

Structure of the fluorescent protein asFP499 from Anemonia sulcata

Summary for 2C9I

• Entry DOI: 10.2210/pdb2c9i/pdb
• Related: 1B9C 1BFP 1C4F 1EMA 1EMB 1EMC 1EME 1EMF 1EMG 1EMK 1EML 1EMM 1F09 1F0B 1G7K 1GFL 1GGX 1H6R 1HCJ 1HUY 1JBY 1JBZ 1JC0 1JC1 1KP5 1KYP 1KYR 1KYS 1MYW 1OXD 1OXE 1OXF 1Q4A 1Q4B 1Q4C 1Q4D 1Q4E 1Q73 1QXT 1QY3 1QYF 1RM9 1RMM 1RMO 1RMP 1RRX 1S6Z 1W7S 1W7T 1W7U 1XA9 1XAE 1XSS 1YJF 1Z1P 1Z1Q 1ZGO 1ZGP 1ZGQ 1ZUX 2A46 2A50 2A52 2A53 2A54 2A56 2B3P 2B3Q 2BTJ 2C9I 2C9J 2EMD 2EMN 2EMO
• Descriptor: GREEN FLUORESCENT PROTEIN ASFP499 (2 entities in total)
• Functional Keywords: fluorescent protein, beta-barrel, bioluminescence, luminescence, luminescent protein
• Biological source: ANEMONIA SULCATA (MEDITERRANEAN SNAKELOCKS SEA ANEMONE)
• Total number of polymer chains: 8
• Total formula weight: 203031.51

Authors

Renzi, F.,Nienhaus, K.,Wiedenmann, J.,Vallone, B.,Nienhaus, G.U. (deposition date: 2005-12-12, release date: 2007-01-16, Last modification date: 2024-10-16)

Primary citation

Nienhaus, K.,Renzi, F.,Vallone, B.,Wiedenmann, J.,Nienhaus, G.U.
Chromophore-Protein Interactions in the Anthozoan Green Fluorescent Protein Asfp499
Biophys.J., 91:4210-, 2006

PubMed Abstract: Despite their similar fold topologies, anthozoan fluorescent proteins (FPs) can exhibit widely different optical properties, arising either from chemical modification of the chromophore itself or from specific interactions of the chromophore with the surrounding protein moiety. Here we present a structural and spectroscopic investigation of the green FP asFP499 from the sea anemone Anemonia sulcata var. rufescens to explore the effects of the protein environment on the chromophore. The optical absorption and fluorescence spectra reveal two discrete species populated in significant proportions over a wide pH range. Moreover, multiple protonation reactions are evident from the observed pH-dependent spectral changes. The x-ray structure of asFP499, determined by molecular replacement at a resolution of 1.85 A, shows the typical beta-barrel fold of the green FP from Aequorea victoria (avGFP). In its center, the chromophore, formed from the tripeptide Gln(63)-Tyr(64)-Gly(65), is tightly held by multiple hydrogen bonds in a polar cage that is structurally quite dissimilar to that of avGFP. The x-ray structure provides interesting clues as to how the spectroscopic properties are fine tuned by the chromophore environment.

PubMed: 16980366
DOI: 10.1529/BIOPHYSJ.106.087411

Experimental method

X-RAY DIFFRACTION (1.82 Å)