2fl1: Difference between revisions
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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== | ||
<StructureSection load='2fl1' size='340' side='right' caption='[[2fl1]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2fl1' size='340' side='right' caption='[[2fl1]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=XYG:[(4Z)-2-[(1Z)-ETHANIMIDOYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>XYG</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=XYG:[(4Z)-2-[(1Z)-ETHANIMIDOYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>XYG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xa9|1xa9]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xa9|1xa9]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fl1 OCA], [http://pdbe.org/2fl1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fl1 RCSB], [http://www.ebi.ac.uk/pdbsum/2fl1 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fl1 OCA], [http://pdbe.org/2fl1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fl1 RCSB], [http://www.ebi.ac.uk/pdbsum/2fl1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fl1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fl/2fl1_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fl/2fl1_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 11:56, 14 June 2018
Crystal structure of red fluorescent protein from Zoanthus, zRFP574, at 2.4A resolutionCrystal structure of red fluorescent protein from Zoanthus, zRFP574, at 2.4A resolution
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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