2g6x: Difference between revisions

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==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==

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[[Category: Pontellina plumata]]

[[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: green fluorescent protein]]

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[[Category: rapid maturation]]

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@@ Line 4: / Line 4: @@
 ==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==
@@ Line 13: / Line 13: @@
 [[Category: Pontellina plumata]]
 [[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: green fluorescent protein]]
@@ Line 21: / Line 21: @@
 [[Category: rapid maturation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:53:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:28:44 2008''