2a46: Difference between revisions

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New page: left|200px<br /><applet load="2a46" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a46, resolution 1.650Å" /> '''Crystal structures ...
 
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[[Image:2a46.gif|left|200px]]<br /><applet load="2a46" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2a46.gif|left|200px]]<br /><applet load="2a46" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2a46, resolution 1.650&Aring;" />
caption="2a46, resolution 1.650&Aring;" />
'''Crystal structures of amFP486, a cyan fluorescent protein from Anemonia majano, and variants'''<br />
'''Crystal structures of amFP486, a cyan fluorescent protein from Anemonia majano, and variants'''<br />


==Overview==
==Overview==
Fluorescent proteins isolated from coral reef organisms can be roughly, grouped into four color classes by emission, cyan, green, yellow, and red., To gain insight into the structural basis for cyan emission, the crystal, structure of amFP486 (lambda(em)max = 486 nm) was determined by molecular, replacement, and the model was refined at 1.65-A resolution. The electron, density map reveals a chromophore formed from the tripeptide sequence, -K-Y-G- that is indistinguishable from that of GFP (lambda(em)max = 509, nm). However, the chromophore environment closely parallels those of the, yellow- and red-shifted homologs zFP538, DsRed, and eqFP611. Mutagenesis, was performed for Glu-150, Ala-165, His-199, and Glu-217, which are, immediately adjacent to the chromophore. His-199 and Ala-165 are key side, chains responsible for the blue shift, presumably by localizing, chromophore charge density on the phenolate moiety. Furthermore, in the, H199T mutant the fluorescence quantum yield is reduced by a factor of, approximately 110. The crystal structures of H199T (lambda(em)max = 515, nm) and E150Q (lambda(em)max = 506 nm) were determined. Remarkably, the, H199T structure reveals that the stacking interaction of His-199 with the, chromophore also controls the fluorescence efficiency, because the, chromophore is statistically distributed in a 1:1 ratio between cis, (fluorescent) and trans (nonfluorescent) conformations.
Fluorescent proteins isolated from coral reef organisms can be roughly grouped into four color classes by emission, cyan, green, yellow, and red. To gain insight into the structural basis for cyan emission, the crystal structure of amFP486 (lambda(em)max = 486 nm) was determined by molecular replacement, and the model was refined at 1.65-A resolution. The electron density map reveals a chromophore formed from the tripeptide sequence -K-Y-G- that is indistinguishable from that of GFP (lambda(em)max = 509 nm). However, the chromophore environment closely parallels those of the yellow- and red-shifted homologs zFP538, DsRed, and eqFP611. Mutagenesis was performed for Glu-150, Ala-165, His-199, and Glu-217, which are immediately adjacent to the chromophore. His-199 and Ala-165 are key side chains responsible for the blue shift, presumably by localizing chromophore charge density on the phenolate moiety. Furthermore, in the H199T mutant the fluorescence quantum yield is reduced by a factor of approximately 110. The crystal structures of H199T (lambda(em)max = 515 nm) and E150Q (lambda(em)max = 506 nm) were determined. Remarkably, the H199T structure reveals that the stacking interaction of His-199 with the chromophore also controls the fluorescence efficiency, because the chromophore is statistically distributed in a 1:1 ratio between cis (fluorescent) and trans (nonfluorescent) conformations.


==About this Structure==
==About this Structure==
2A46 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anemonia_majano Anemonia majano] with BME as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A46 OCA].  
2A46 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anemonia_majano Anemonia majano] with <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A46 OCA].  


==Reference==
==Reference==
Line 13: Line 13:
[[Category: Anemonia majano]]
[[Category: Anemonia majano]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Henderson, J.N.]]
[[Category: Henderson, J N.]]
[[Category: Remington, S.J.]]
[[Category: Remington, S J.]]
[[Category: BME]]
[[Category: BME]]
[[Category: beta barrel]]
[[Category: beta barrel]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:23:26 2008''

Revision as of 17:23, 21 February 2008

File:2a46.gif


2a46, resolution 1.650Å

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Crystal structures of amFP486, a cyan fluorescent protein from Anemonia majano, and variants

OverviewOverview

Fluorescent proteins isolated from coral reef organisms can be roughly grouped into four color classes by emission, cyan, green, yellow, and red. To gain insight into the structural basis for cyan emission, the crystal structure of amFP486 (lambda(em)max = 486 nm) was determined by molecular replacement, and the model was refined at 1.65-A resolution. The electron density map reveals a chromophore formed from the tripeptide sequence -K-Y-G- that is indistinguishable from that of GFP (lambda(em)max = 509 nm). However, the chromophore environment closely parallels those of the yellow- and red-shifted homologs zFP538, DsRed, and eqFP611. Mutagenesis was performed for Glu-150, Ala-165, His-199, and Glu-217, which are immediately adjacent to the chromophore. His-199 and Ala-165 are key side chains responsible for the blue shift, presumably by localizing chromophore charge density on the phenolate moiety. Furthermore, in the H199T mutant the fluorescence quantum yield is reduced by a factor of approximately 110. The crystal structures of H199T (lambda(em)max = 515 nm) and E150Q (lambda(em)max = 506 nm) were determined. Remarkably, the H199T structure reveals that the stacking interaction of His-199 with the chromophore also controls the fluorescence efficiency, because the chromophore is statistically distributed in a 1:1 ratio between cis (fluorescent) and trans (nonfluorescent) conformations.

About this StructureAbout this Structure

2A46 is a Single protein structure of sequence from Anemonia majano with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures and mutational analysis of amFP486, a cyan fluorescent protein from Anemonia majano., Henderson JN, Remington SJ, Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12712-7. Epub 2005 Aug 24. PMID:16120682

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