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{{STRUCTURE_2fl1| PDB=2fl1 | SCENE= }} | |||
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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]] | ||
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Revision as of 04:01, 4 May 2008
Crystal structure of red fluorescent protein from Zoanthus, zRFP574, at 2.4A resolution
OverviewOverview
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 StructureAbout this Structure
2FL1 is a Single protein structure of sequence from Zoanthus sp.. Full crystallographic information is available from OCA.
ReferenceReference
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
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- 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