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New page: left|200px<br /><applet load="2fl1" size="350" color="white" frame="true" align="right" spinBox="true" caption="2fl1, resolution 2.4Å" /> '''Crystal structure of ...
 
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==Overview==
==Overview==
The three-dimensional structure of the red fluorescent protein (RFP), zRFP574 from the button polyp Zoanthus sp. (two dimers per asymmetric, unit, 231 x 4 amino acids) has been determined at 2.4 A resolution in, space group C222(1). The crystal structure, refined to a crystallographic, R factor of 0.203 (R(free) = 0.249), adopts the beta-barrel fold composed, of 11 strands similar to that of the yellow fluorescent protein zYFP538., The zRFP574 chromophore, originating from the protein sequence, Asp66-Tyr67-Gly68, has a two-ring structure typical of GFP-like proteins., The bond geometry of residue 66 shows the strong tendency of the, corresponding C(alpha) atom to sp(2) hybridization as a consequence of, N-acylimine bond formation. The zRFP574 chromophore contains the 65-66, cis-peptide bond characteristic of red fluorescent proteins. The, chromophore phenolic ring adopts a cis conformation coplanar with the, imidazolinone ring. The crystallographic study has revealed an unexpected, chemical feature of the internal chromophore. A decarboxylated side chain, of the chromophore-forming residue Asp66 has been observed in the, structure. This additional post-translational modification is likely to, play a key role in the bathochromic shift of the zRFP574 spectrum.
The three-dimensional structure of the red fluorescent protein (RFP) zRFP574 from the button polyp Zoanthus sp. (two dimers per asymmetric unit, 231 x 4 amino acids) has been determined at 2.4 A resolution in space group C222(1). The crystal structure, refined to a crystallographic R factor of 0.203 (R(free) = 0.249), adopts the beta-barrel fold composed of 11 strands similar to that of the yellow fluorescent protein zYFP538. The zRFP574 chromophore, originating from the protein sequence Asp66-Tyr67-Gly68, has a two-ring structure typical of GFP-like proteins. The bond geometry of residue 66 shows the strong tendency of the corresponding C(alpha) atom to sp(2) hybridization as a consequence of N-acylimine bond formation. The zRFP574 chromophore contains the 65-66 cis-peptide bond characteristic of red fluorescent proteins. The chromophore phenolic ring adopts a cis conformation coplanar with the imidazolinone ring. The crystallographic study has revealed an unexpected chemical feature of the internal chromophore. A decarboxylated side chain of the chromophore-forming residue Asp66 has been observed in the structure. This additional post-translational modification is likely to play a key role in the bathochromic shift of the zRFP574 spectrum.


==About this Structure==
==About this Structure==
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[[Category: zrfp574]]
[[Category: zrfp574]]


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Revision as of 15:22, 21 February 2008

File:2fl1.jpg


2fl1, resolution 2.4Å

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Crystal structure of red fluorescent protein from Zoanthus, zRFP574, at 2.4A resolution

Overview

The three-dimensional structure of the red fluorescent protein (RFP) zRFP574 from the button polyp Zoanthus sp. (two dimers per asymmetric unit, 231 x 4 amino acids) has been determined at 2.4 A resolution in space group C222(1). The crystal structure, refined to a crystallographic R factor of 0.203 (R(free) = 0.249), adopts the beta-barrel fold composed of 11 strands similar to that of the yellow fluorescent protein zYFP538. The zRFP574 chromophore, originating from the protein sequence Asp66-Tyr67-Gly68, has a two-ring structure typical of GFP-like proteins. The bond geometry of residue 66 shows the strong tendency of the corresponding C(alpha) atom to sp(2) hybridization as a consequence of N-acylimine bond formation. The zRFP574 chromophore contains the 65-66 cis-peptide bond characteristic of red fluorescent proteins. The chromophore phenolic ring adopts a cis conformation coplanar with the imidazolinone ring. The crystallographic study has revealed an unexpected chemical feature of the internal chromophore. A decarboxylated side chain of the chromophore-forming residue Asp66 has been observed in the structure. This additional post-translational modification is likely to play a key role in the bathochromic shift of the zRFP574 spectrum.

About this Structure

2FL1 is a Single protein structure of sequence from Zoanthus sp. with SO4 as ligand. Full crystallographic information is available from OCA.

Reference

Structure of a red fluorescent protein from Zoanthus, zRFP574, reveals a novel chromophore., Pletneva N, Pletnev S, Tikhonova T, Popov V, Martynov V, Pletnev V, Acta Crystallogr D Biol Crystallogr. 2006 May;62(Pt 5):527-32. Epub 2006, Apr 19. PMID:16627946

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