1q73: Difference between revisions
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==S65T Q80R Y145C T203C Green Fluorescent Protein (GFP) pH 8.5== | ==S65T Q80R Y145C T203C Green Fluorescent Protein (GFP) pH 8.5== | ||
<StructureSection load='1q73' size='340' side='right' caption='[[1q73]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1q73' size='340' side='right' caption='[[1q73]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q4a|1q4a]], [[1q4b|1q4b]], [[1q4c|1q4c]], [[1q4d|1q4d]], [[1q4e|1q4e]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q4a|1q4a]], [[1q4b|1q4b]], [[1q4c|1q4c]], [[1q4d|1q4d]], [[1q4e|1q4e]]</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=1q73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q73 OCA], [http://pdbe.org/1q73 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q73 RCSB], [http://www.ebi.ac.uk/pdbsum/1q73 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=1q73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q73 OCA], [http://pdbe.org/1q73 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q73 RCSB], [http://www.ebi.ac.uk/pdbsum/1q73 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q73 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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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/q7/1q73_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q7/1q73_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> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1q73" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1q73" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 11:31, 24 February 2018
S65T Q80R Y145C T203C Green Fluorescent Protein (GFP) pH 8.5S65T Q80R Y145C T203C Green Fluorescent Protein (GFP) pH 8.5
Structural highlights
Function[GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. 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 PubMedAtomic resolution structures of proteins indicate that the core is typically well packed, suggesting a densely connected network of interactions between amino acid residues. The combinatorial complexity of energetic interactions in such a network could be enormous, a problem that limits our ability to relate structure and function. Here, we report a case study of the complexity of amino acid interactions in a localized region within the core of the GFP, a particularly stable and tightly packed molecule. Mutations at three sites within the chromophore-binding pocket display an overlapping pattern of conformational change and are thermodynamically coupled, seemingly consistent with the dense network model. However, crystallographic and energetic analyses of coupling between mutations paint a different picture; pairs of mutations couple through independent "hotspots" in the region of structural overlap. The data indicate that, even in highly stable proteins, the core contains sufficient plasticity in packing to uncouple high-order energetic interactions of residues, a property that is likely general in proteins. Local complexity of amino acid interactions in a protein core.,Jain RK, Ranganathan R Proc Natl Acad Sci U S A. 2004 Jan 6;101(1):111-6. Epub 2003 Dec 18. PMID:14684834[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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