2fl1: Difference between revisions

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[[Image:2fl1.jpg|left|200px]]
{{Seed}}
[[Image:2fl1.png|left|200px]]


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{{STRUCTURE_2fl1|  PDB=2fl1  |  SCENE=  }}  
{{STRUCTURE_2fl1|  PDB=2fl1  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_16627946}}


==About this Structure==
==About this Structure==
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[[Category: Zoanthus sp.]]
[[Category: Zoanthus sp.]]
[[Category: Zrfp574]]
[[Category: Zrfp574]]
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