2C9J

Structure of the fluorescent protein cmFP512 at 1.35A from Cerianthus membranaceus

2C9J の概要

• エントリーDOI: 10.2210/pdb2c9j/pdb
• 関連するPDBエントリー: 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 2EMD 2EMN 2EMO
• 分子名称: GREEN FLUORESCENT PROTEIN FP512 (2 entities in total)
• 機能のキーワード: fluorescent protein, beta-barrel, bioluminescence, luminescence, luminescent protein
• 由来する生物種: CERIANTHUS MEMBRANACEUS
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 202677.94

構造登録者

Renzi, F.,Nienhaus, K.,Wiedenmann, J.,Vallone, B.,Nienhaus, G.U. (登録日: 2005-12-12, 公開日: 2006-10-30, 最終更新日: 2024-11-13)

主引用文献

Nienhaus, K.,Renzi, F.,Vallone, B.,Wiedenmann, J.,Nienhaus, G.U.
Exploring Chromophore-Protein Interactions in Fluorescent Protein Cmfp512 from Cerianthus Membranaceus: X-Ray Structure Analysis and Optical Spectroscopy.
Biochemistry, 45:12492-, 2006

PubMed Abstract: Autofluorescent proteins of the GFP family all share the same three-dimensional beta-can fold; yet they 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 characterization of the green fluorescent protein cmFP512 from Cerianthus membranaceus, a nonbioluminescent, azooxanthellate cnidarian, which has only approximately 22% sequence identity with Aequorea victoria GFP. The X-ray structure, obtained by molecular replacement at a resolution of 1. 35 A, shows the chromophore, formed from the tripeptide Gln-Tyr-Gly, in a hydrogen-bonded cage in the center of an 11-stranded beta-barrel, tightly restrained by adjacent residues and structural water molecules. It exists in a neutral (A) and an anionic (B) species, with absorption/emission maxima at 392/460 (pH 5) and 503/512 nm (pH 7). Their fractional populations and peak positions depend sensitively on pH, reflecting protonation of groups adjacent to the chromophore. The pH dependence of the spectra is explained by a protonation mechanism involving a hydrogen-bonded cluster of charged/polar groups. Cryospectroscopy at 12 K was also performed to analyze the vibronic coupling of the electronic transitions.

PubMed: 17059211
DOI: 10.1021/BI060885C

実験手法

X-RAY DIFFRACTION (1.35 Å)