4kf5: Difference between revisions
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==Crystal Structure of Split GFP complexed with engineered sfCherry with an insertion of GFP fragment== | ==Crystal Structure of Split GFP complexed with engineered sfCherry with an insertion of GFP fragment== | ||
<StructureSection load='4kf5' size='340' side='right' caption='[[4kf5]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='4kf5' size='340' side='right' caption='[[4kf5]], [[Resolution|resolution]] 2.60Å' 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=CH6:{(4Z)-2-[(1S)-1-AMINO-3-(METHYLSULFANYL)PROPYL]-4-[(4-HYDROXYPHENYL)METHYLIDENE]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CH6</scene>, <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=CH6:{(4Z)-2-[(1S)-1-AMINO-3-(METHYLSULFANYL)PROPYL]-4-[(4-HYDROXYPHENYL)METHYLIDENE]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CH6</scene>, <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">[[4kf4|4kf4]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kf4|4kf4]]</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=4kf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kf5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kf5 RCSB], [http://www.ebi.ac.uk/pdbsum/4kf5 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=4kf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kf5 OCA], [http://pdbe.org/4kf5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kf5 RCSB], [http://www.ebi.ac.uk/pdbsum/4kf5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kf5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4kf5" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 13:51, 5 August 2016
Crystal Structure of Split GFP complexed with engineered sfCherry with an insertion of GFP fragmentCrystal Structure of Split GFP complexed with engineered sfCherry with an insertion of GFP fragment
Structural highlights
Publication Abstract from PubMedA modular strategy for protein crystallization using split green fluorescent protein (GFP) as a crystallization partner is demonstrated. Insertion of a hairpin containing GFP beta-strands 10 and 11 into a surface loop of a target protein provides two chain crossings between the target and the reconstituted GFP compared with the single connection afforded by terminal GFP fusions. This strategy was tested by inserting this hairpin into a loop of another fluorescent protein, sfCherry. The crystal structure of the sfCherry-GFP(10-11) hairpin in complex with GFP(1-9) was determined at a resolution of 2.6 A. Analysis of the complex shows that the reconstituted GFP is attached to the target protein (sfCherry) in a structurally ordered way. This work opens the way to rapidly creating crystallization variants by reconstituting a target protein bearing the GFP(10-11) hairpin with a variety of GFP(1-9) mutants engineered for favorable crystallization. Split green fluorescent protein as a modular binding partner for protein crystallization.,Nguyen HB, Hung LW, Yeates TO, Terwilliger TC, Waldo GS Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2513-23. doi:, 10.1107/S0907444913024608. Epub 2013 Nov 19. PMID:24311592[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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