1yzw
From Proteopedia
(New page: 200px<br /><applet load="1yzw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yzw, resolution 2.10Å" /> '''The 2.1A Crystal Str...) |
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| - | [[Image:1yzw.gif|left|200px]]<br /><applet load="1yzw" size=" | + | [[Image:1yzw.gif|left|200px]]<br /><applet load="1yzw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yzw, resolution 2.10Å" /> | caption="1yzw, resolution 2.10Å" /> | ||
'''The 2.1A Crystal Structure of the Far-red Fluorescent Protein HcRed: Inherent Conformational Flexibility of the Chromophore'''<br /> | '''The 2.1A Crystal Structure of the Far-red Fluorescent Protein HcRed: Inherent Conformational Flexibility of the Chromophore'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have determined the crystal structure of HcRed, a far-red fluorescent | + | 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== | ==About this Structure== | ||
| - | 1YZW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Heteractis_crispa Heteractis crispa] with PEG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1YZW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Heteractis_crispa Heteractis crispa] with <scene name='pdbligand=PEG:'>PEG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YZW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Heteractis crispa]] | [[Category: Heteractis crispa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Buckle, A | + | [[Category: Buckle, A M.]] |
| - | [[Category: Devenish, R | + | [[Category: Devenish, R J.]] |
[[Category: Petersen, J.]] | [[Category: Petersen, J.]] | ||
[[Category: Pettikiriarachchi, A.]] | [[Category: Pettikiriarachchi, A.]] | ||
[[Category: Prescott, M.]] | [[Category: Prescott, M.]] | ||
[[Category: Rossjohn, J.]] | [[Category: Rossjohn, J.]] | ||
| - | [[Category: Wilmann, P | + | [[Category: Wilmann, P G.]] |
[[Category: PEG]] | [[Category: PEG]] | ||
[[Category: luminescent protein]] | [[Category: luminescent protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:49 2008'' |
Revision as of 14:10, 21 February 2008
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The 2.1A Crystal Structure of the Far-red Fluorescent Protein HcRed: Inherent Conformational Flexibility of the Chromophore
Overview
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
1YZW is a Single protein structure of sequence from Heteractis crispa with as ligand. Full crystallographic information is available from OCA.
Reference
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
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