1zux: Difference between revisions

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New page: left|200px<br /><applet load="1zux" size="350" color="white" frame="true" align="right" spinBox="true" caption="1zux, resolution 1.850Å" /> '''EosFP Fluorescent P...
 
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==Overview==
==Overview==
Genetically encoded fusion constructs derived from fluorescent proteins, (FPs) can be designed to report on a multitude of events and signals in, cells, tissues, and entire organs without interfering with the complex, machinery of life. EosFP is a novel FP from the scleractinian coral, Lobophyllia hemprichii that switches its fluorescence emission from green, (516 nm) to red (581 nm) upon irradiation with approximately 400-nm light., This property enables localized tagging of proteins and thus provides a, valuable tool for tracking protein movements within live cells. Here, we, present the x-ray structures of the green and red forms of WT EosFP. They, reveal that formation of the red chromophore is associated with cleavage, of the peptide backbone, with surprisingly little change elsewhere in the, structure, and provide insights into the mechanism that generates this, interesting posttranslational polypeptide modification.
Genetically encoded fusion constructs derived from fluorescent proteins (FPs) can be designed to report on a multitude of events and signals in cells, tissues, and entire organs without interfering with the complex machinery of life. EosFP is a novel FP from the scleractinian coral Lobophyllia hemprichii that switches its fluorescence emission from green (516 nm) to red (581 nm) upon irradiation with approximately 400-nm light. This property enables localized tagging of proteins and thus provides a valuable tool for tracking protein movements within live cells. Here, we present the x-ray structures of the green and red forms of WT EosFP. They reveal that formation of the red chromophore is associated with cleavage of the peptide backbone, with surprisingly little change elsewhere in the structure, and provide insights into the mechanism that generates this interesting posttranslational polypeptide modification.


==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Nar, H.]]
[[Category: Nar, H.]]
[[Category: Nienhaus, G.U.]]
[[Category: Nienhaus, G U.]]
[[Category: Nienhaus, K.]]
[[Category: Nienhaus, K.]]
[[Category: Wiedenmann, J.]]
[[Category: Wiedenmann, J.]]
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[[Category: photoconversion]]
[[Category: photoconversion]]


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Revision as of 17:19, 21 February 2008

File:1zux.gif


1zux, resolution 1.850Å

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EosFP Fluorescent Protein- Green Form

OverviewOverview

Genetically encoded fusion constructs derived from fluorescent proteins (FPs) can be designed to report on a multitude of events and signals in cells, tissues, and entire organs without interfering with the complex machinery of life. EosFP is a novel FP from the scleractinian coral Lobophyllia hemprichii that switches its fluorescence emission from green (516 nm) to red (581 nm) upon irradiation with approximately 400-nm light. This property enables localized tagging of proteins and thus provides a valuable tool for tracking protein movements within live cells. Here, we present the x-ray structures of the green and red forms of WT EosFP. They reveal that formation of the red chromophore is associated with cleavage of the peptide backbone, with surprisingly little change elsewhere in the structure, and provide insights into the mechanism that generates this interesting posttranslational polypeptide modification.

About this StructureAbout this Structure

1ZUX is a Single protein structure of sequence from Lobophyllia hemprichii. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP., Nienhaus K, Nienhaus GU, Wiedenmann J, Nar H, Proc Natl Acad Sci U S A. 2005 Jun 28;102(26):9156-9. Epub 2005 Jun 17. PMID:15964985

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