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[[Image:1yzw.gif|left|200px]]
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{{STRUCTURE_1yzw|  PDB=1yzw  |  SCENE=  }}
'''The 2.1A Crystal Structure of the Far-red Fluorescent Protein HcRed: Inherent Conformational Flexibility of the Chromophore'''


==The 2.1A Crystal Structure of the Far-red Fluorescent Protein HcRed: Inherent Conformational Flexibility of the Chromophore==
<StructureSection load='1yzw' size='340' side='right'caption='[[1yzw]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1yzw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Radianthus_crispa Radianthus crispa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YZW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRU:4-[(4Z)-1-(CARBOXYMETHYL)-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-2-YL]-4-IMINOBUTANOIC+ACID'>CRU</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yzw OCA], [https://pdbe.org/1yzw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yzw RCSB], [https://www.ebi.ac.uk/pdbsum/1yzw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yzw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NFCP_RADCR NFCP_RADCR]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yz/1yzw_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1yzw ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have determined the crystal structure of HcRed, a far-red fluorescent protein isolated from Heteractis crispa, to 2.1A resolution. HcRed was observed to form a dimer, in contrast to the monomeric form of green fluorescent protein (GFP) or the tetrameric forms of the GFP-like proteins (eqFP611, Rtms5 and DsRed). Unlike the well-defined chromophore conformation observed in GFP and the GFP-like proteins, the HcRed chromophore was observed to be considerably mobile. Within the HcRed structure, the cyclic tripeptide chromophore, Glu(64)-Tyr(65)-Gly(66), was observed to adopt both a cis coplanar and a trans non-coplanar conformation. As a result of these two conformations, the hydroxyphenyl moiety of the chromophore makes distinct interactions within the interior of the beta-can. These data together with a quantum chemical model of the chromophore, suggest the cis coplanar conformation to be consistent with the fluorescent properties of HcRed, and the trans non-coplanar conformation to be consistent with non-fluorescent properties of hcCP, the chromoprotein parent of HcRed. Moreover, within the GFP-like family, it appears that where conformational freedom is permissible then flexibility in the chromophore conformation is possible.


==Overview==
The 2.1A crystal structure of the far-red fluorescent protein HcRed: inherent conformational flexibility of the chromophore.,Wilmann PG, Petersen J, Pettikiriarachchi A, Buckle AM, Smith SC, Olsen S, Perugini MA, Devenish RJ, Prescott M, Rossjohn J J Mol Biol. 2005 May 27;349(1):223-37. Epub 2005 Mar 22. PMID:15876379<ref>PMID:15876379</ref>
We have determined the crystal structure of HcRed, a far-red fluorescent protein isolated from Heteractis crispa, to 2.1A resolution. HcRed was observed to form a dimer, in contrast to the monomeric form of green fluorescent protein (GFP) or the tetrameric forms of the GFP-like proteins (eqFP611, Rtms5 and DsRed). Unlike the well-defined chromophore conformation observed in GFP and the GFP-like proteins, the HcRed chromophore was observed to be considerably mobile. Within the HcRed structure, the cyclic tripeptide chromophore, Glu(64)-Tyr(65)-Gly(66), was observed to adopt both a cis coplanar and a trans non-coplanar conformation. As a result of these two conformations, the hydroxyphenyl moiety of the chromophore makes distinct interactions within the interior of the beta-can. These data together with a quantum chemical model of the chromophore, suggest the cis coplanar conformation to be consistent with the fluorescent properties of HcRed, and the trans non-coplanar conformation to be consistent with non-fluorescent properties of hcCP, the chromoprotein parent of HcRed. Moreover, within the GFP-like family, it appears that where conformational freedom is permissible then flexibility in the chromophore conformation is possible.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1YZW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Heteractis_crispa Heteractis crispa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YZW OCA].
</div>
<div class="pdbe-citations 1yzw" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
The 2.1A crystal structure of the far-red fluorescent protein HcRed: inherent conformational flexibility of the chromophore., Wilmann PG, Petersen J, Pettikiriarachchi A, Buckle AM, Smith SC, Olsen S, Perugini MA, Devenish RJ, Prescott M, Rossjohn J, J Mol Biol. 2005 May 27;349(1):223-37. Epub 2005 Mar 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15876379 15876379]
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
[[Category: Heteractis crispa]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Buckle, A M.]]
__TOC__
[[Category: Devenish, R J.]]
</StructureSection>
[[Category: Petersen, J.]]
[[Category: Large Structures]]
[[Category: Pettikiriarachchi, A.]]
[[Category: Radianthus crispa]]
[[Category: Prescott, M.]]
[[Category: Buckle AM]]
[[Category: Rossjohn, J.]]
[[Category: Devenish RJ]]
[[Category: Wilmann, P G.]]
[[Category: Petersen J]]
[[Category: Luminescent protein]]
[[Category: Pettikiriarachchi A]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:00:56 2008''
[[Category: Prescott M]]
[[Category: Rossjohn J]]
[[Category: Wilmann PG]]

Latest revision as of 07:43, 30 October 2024

The 2.1A Crystal Structure of the Far-red Fluorescent Protein HcRed: Inherent Conformational Flexibility of the Chromophore

1yzw, resolution 2.10Å

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