2g6y: Difference between revisions

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New page: left|200px<br /><applet load="2g6y" size="350" color="white" frame="true" align="right" spinBox="true" caption="2g6y, resolution 1.600Å" /> '''Crystal structure o...
 
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==Overview==
==Overview==
Since the cloning of Aequorea victoria green fluorescent protein (GFP) in, 1992, a family of known GFP-like proteins has been growing rapidly. Today, it includes more than a hundred proteins with different spectral, characteristics cloned from Cnidaria species. For some of these proteins, crystal structures have been solved, showing diversity in chromophore, modifications and conformational states. However, we are still far from a, complete understanding of the origin, functions and evolution of the GFP, family. Novel proteins of the family were recently cloned from, evolutionarily distant marine Copepoda species, phylum Arthropoda, demonstrating an extremely rapid generation of fluorescent signal. Here, we have generated a non-aggregating mutant of Copepoda fluorescent protein, and solved its high-resolution crystal structure. It was found that the, protein beta-barrel contains a pore, leading to the chromophore. Using, site-directed mutagenesis, we showed that this feature is critical for the, fast maturation of the chromophore.
Since the cloning of Aequorea victoria green fluorescent protein (GFP) in 1992, a family of known GFP-like proteins has been growing rapidly. Today, it includes more than a hundred proteins with different spectral characteristics cloned from Cnidaria species. For some of these proteins, crystal structures have been solved, showing diversity in chromophore modifications and conformational states. However, we are still far from a complete understanding of the origin, functions and evolution of the GFP family. Novel proteins of the family were recently cloned from evolutionarily distant marine Copepoda species, phylum Arthropoda, demonstrating an extremely rapid generation of fluorescent signal. Here, we have generated a non-aggregating mutant of Copepoda fluorescent protein and solved its high-resolution crystal structure. It was found that the protein beta-barrel contains a pore, leading to the chromophore. Using site-directed mutagenesis, we showed that this feature is critical for the fast maturation of the chromophore.


==About this Structure==
==About this Structure==
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[[Category: Pontellina plumata]]
[[Category: Pontellina plumata]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chudakov, D.M.]]
[[Category: Chudakov, D M.]]
[[Category: Evdokimov, A.G.]]
[[Category: Evdokimov, A G.]]
[[Category: Pokross, M.E.]]
[[Category: Pokross, M E.]]
[[Category: beta-can]]
[[Category: beta-can]]
[[Category: green fluorescent protein]]
[[Category: green fluorescent protein]]
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[[Category: rapid maturation]]
[[Category: rapid maturation]]


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Revision as of 18:28, 21 February 2008

File:2g6y.gif


2g6y, resolution 1.600Å

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Crystal structure of the novel green fluorescent protein from marine copepod Pontellina plumata

OverviewOverview

Since the cloning of Aequorea victoria green fluorescent protein (GFP) in 1992, a family of known GFP-like proteins has been growing rapidly. Today, it includes more than a hundred proteins with different spectral characteristics cloned from Cnidaria species. For some of these proteins, crystal structures have been solved, showing diversity in chromophore modifications and conformational states. However, we are still far from a complete understanding of the origin, functions and evolution of the GFP family. Novel proteins of the family were recently cloned from evolutionarily distant marine Copepoda species, phylum Arthropoda, demonstrating an extremely rapid generation of fluorescent signal. Here, we have generated a non-aggregating mutant of Copepoda fluorescent protein and solved its high-resolution crystal structure. It was found that the protein beta-barrel contains a pore, leading to the chromophore. Using site-directed mutagenesis, we showed that this feature is critical for the fast maturation of the chromophore.

About this StructureAbout this Structure

2G6Y is a Single protein structure of sequence from Pontellina plumata. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the fast maturation of Arthropoda green fluorescent protein., Evdokimov AG, Pokross ME, Egorov NS, Zaraisky AG, Yampolsky IV, Merzlyak EM, Shkoporov AN, Sander I, Lukyanov KA, Chudakov DM, EMBO Rep. 2006 Oct;7(10):1006-12. Epub 2006 Aug 25. PMID:16936637

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