6l27
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==X-ray crystal structure of the mutant green fluorescent protein== | |
+ | <StructureSection load='6l27' size='340' side='right'caption='[[6l27]], [[Resolution|resolution]] 0.77Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6l27]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L27 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6L27 FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene></td></tr> | ||
+ | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GYS:[(4Z)-2-(1-AMINO-2-HYDROXYETHYL)-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>GYS</scene></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=6l27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l27 OCA], [http://pdbe.org/6l27 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l27 RCSB], [http://www.ebi.ac.uk/pdbsum/6l27 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l27 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://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;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Neutron crystallography has been used to elucidate the protonation states for the enhanced green fluorescent protein, which has revolutionized imaging technologies. The structure has a deprotonated hydroxyl group in the fluorescent chromophore. Also, the protonation states of His148 and Thr203, as well as the orientation of a critical water molecule in direct contact with the chromophore, could be determined. The results demonstrate that the deprotonated hydroxyl group in the chromophore and the nitrogen atom ND1 in His148 are charged negatively and positively, respectively, forming an ion pair. The position of the two deuterium atoms in the critical water molecule appears to be displaced slightly toward the acceptor oxygen atoms according to their omit maps. This displacement implies the formation of an intriguing electrostatic potential realized inside of the protein. Our findings provide new insights into future protein design strategies along with developments in quantum chemical calculations. | ||
- | + | Direct Observation of the Protonation States in the Mutant Green Fluorescent Protein.,Shibazaki C, Shimizu R, Kagotani Y, Ostermann A, Schrader TE, Adachi M J Phys Chem Lett. 2020 Jan 16;11(2):492-496. doi: 10.1021/acs.jpclett.9b03252., Epub 2020 Jan 6. PMID:31880458<ref>PMID:31880458</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 6l27" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Adachi, M]] | ||
+ | [[Category: Kagotani, Y]] | ||
+ | [[Category: Ostermann, A]] | ||
+ | [[Category: Schrader, T E]] | ||
+ | [[Category: Shibazaki, C]] | ||
+ | [[Category: Shimizu, R]] | ||
+ | [[Category: Fluorescent protein]] | ||
+ | [[Category: Gfp]] | ||
+ | [[Category: Mutant]] | ||
+ | [[Category: Recombinant]] |
Revision as of 09:08, 1 April 2020
X-ray crystal structure of the mutant green fluorescent protein
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