Publication Date:
1996-09-06
Description:
The green fluorescent protein (GFP) from the Pacific Northwest jellyfish Aequorea victoria has generated intense interest as a marker for gene expression and localization of gene products. The chromophore, resulting from the spontaneous cyclization and oxidation of the sequence -Ser65 (or Thr65)-Tyr66-Gly67-, requires the native protein fold for both formation and fluorescence emission. The structure of Thr65 GFP has been determined at 1.9 angstrom resolution. The protein fold consists of an 11-stranded beta barrel with a coaxial helix, with the chromophore forming from the central helix. Directed mutagenesis of one residue adjacent to the chromophore, Thr203, to Tyr or His results in significantly red-shifted excitation and emission maxima.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ormo, M -- Cubitt, A B -- Kallio, K -- Gross, L A -- Tsien, R Y -- Remington, S J -- New York, N.Y. -- Science. 1996 Sep 6;273(5280):1392-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Department of Physics, University of Oregon, Eugene, OR 97403-1226, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703075" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Crystallography, X-Ray
;
Green Fluorescent Proteins
;
Hydrogen Bonding
;
Luminescent Proteins/*chemistry/genetics
;
Models, Molecular
;
Molecular Sequence Data
;
Mutagenesis, Site-Directed
;
*Protein Conformation
;
Protein Folding
;
Protein Structure, Secondary
;
Spectrometry, Fluorescence
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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