2fl1
From Proteopedia
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'''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''' | ||
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[[Category: Popov, B.]] | [[Category: Popov, B.]] | ||
[[Category: Tikhonova, T.]] | [[Category: Tikhonova, T.]] | ||
- | [[Category: | + | [[Category: Beta barrel]] |
- | [[Category: | + | [[Category: Beta-can fold]] |
- | [[Category: | + | [[Category: Button polyp]] |
- | [[Category: | + | [[Category: Chromophore]] |
- | [[Category: | + | [[Category: Crystal structure]] |
- | [[Category: | + | [[Category: Emission maximum 574nm]] |
- | [[Category: | + | [[Category: Fluorescent marker]] |
- | [[Category: | + | [[Category: Intersubunit interface]] |
- | [[Category: | + | [[Category: Red fluorescent protein]] |
- | [[Category: | + | [[Category: Tightly packed tetramer]] |
- | [[Category: | + | [[Category: Zoanthus sp.]] |
- | [[Category: | + | [[Category: Zrfp574]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:00:59 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 01:01, 4 May 2008
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.. 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 Page seeded by OCA on Sun May 4 04:00:59 2008
Categories: Single protein | Zoanthus sp. | Martynov, V. | Pletnev, S. | Pletnev, V. | Pletneva, N. | Popov, B. | Tikhonova, T. | Beta barrel | Beta-can fold | Button polyp | Chromophore | Crystal structure | Emission maximum 574nm | Fluorescent marker | Intersubunit interface | Red fluorescent protein | Tightly packed tetramer | Zrfp574