4ges: Difference between revisions
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<StructureSection load='4ges' size='340' side='right'caption='[[4ges]], [[Resolution|resolution]] 1.23Å' scene=''> | <StructureSection load='4ges' size='340' side='right'caption='[[4ges]], [[Resolution|resolution]] 1.23Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ges]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ges]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GES FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0WZ:3-(1H-PYRAZOL-1-YL)-L-TYROSINE'>0WZ</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=4ges FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ges OCA], [https://pdbe.org/4ges PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ges RCSB], [https://www.ebi.ac.uk/pdbsum/4ges PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ges ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/GFP_AEQVI 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. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 20: | ||
==See Also== | ==See Also== | ||
*[[Green Fluorescent Protein|Green Fluorescent Protein]] | *[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Aequorea victoria]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Dong | [[Category: Dong J]] | ||
[[Category: Gong | [[Category: Gong W]] | ||
[[Category: Li | [[Category: Li J]] | ||
[[Category: Liu | [[Category: Liu X]] | ||
[[Category: Wang | [[Category: Wang J]] | ||
Revision as of 09:53, 26 October 2022
crystal structure of GFP-TYR151PYZ with an unnatural amino acid incorporationcrystal structure of GFP-TYR151PYZ with an unnatural amino acid incorporation
Structural highlights
FunctionGFP_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. Publication Abstract from PubMedET encounters jellyfish: Through the incorporation of the metal-chelating amino acid pyTyr into green fluorescent protein (GFP) from jellyfish, photoinduced electron transfer (ET) from the GFP chromophore to a bound Cu(II) ion was shown to occur within one nanosecond in a distance-dependent manner. The crystal structure of GFP with pyTyr at a specific position shows the structural basis for the nanomolar binding affinity of pyTyr to Cu(II) ions. Genetic incorporation of a metal-chelating amino Acid as a probe for protein electron transfer.,Liu X, Li J, Dong J, Hu C, Gong W, Wang J Angew Chem Int Ed Engl. 2012 Oct 8;51(41):10261-5. doi: 10.1002/anie.201204962., Epub 2012 Aug 31. PMID:22936654[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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