4w7c

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==Crystal Structure of Full-Length Split GFP Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, C 2 Space Group==
==Crystal Structure of Full-Length Split GFP Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, C 2 Space Group==
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<StructureSection load='4w7c' size='340' side='right' caption='[[4w7c]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='4w7c' size='340' side='right'caption='[[4w7c]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4w7c]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W7C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4W7C FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4w7c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4W7C FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4w6a|4w6a]], [[4w6b|4w6b]], [[4w6c|4w6c]], [[4w6d|4w6d]], [[4w6f|4w6f]], [[4w6g|4w6g]], [[4w6h|4w6h]], [[4w6i|4w6i]], [[4w6j|4w6j]], [[4w6k|4w6k]], [[4w6l|4w6l]], [[4w6m|4w6m]], [[4w6n|4w6n]], [[4w6o|4w6o]], [[4w6p|4w6p]], [[4w6r|4w6r]], [[4w6s|4w6s]], [[4w6t|4w6t]], [[4w6u|4w6u]], [[4w72|4w72]], [[4w73|4w73]], [[4w74|4w74]], [[4w75|4w75]], [[4w76|4w76]], [[4w77|4w77]], [[4w7a|4w7a]], [[4w69|4w69]], [[4w7d|4w7d]], [[4w7e|4w7e]], [[4w7f|4w7f]], [[4w7r|4w7r]], [[4w7x|4w7x]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4w7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w7c OCA], [https://pdbe.org/4w7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4w7c RCSB], [https://www.ebi.ac.uk/pdbsum/4w7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4w7c ProSAT]</span></td></tr>
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<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=4w7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w7c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4w7c RCSB], [http://www.ebi.ac.uk/pdbsum/4w7c PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Applications ranging from synthetic biology to protein crystallization could be advanced by facile systems for connecting multiple proteins together in predefined spatial relationships. One approach to this goal is to engineer many distinct assembly forms of a single carrier protein or scaffold, to which other proteins of interest can then be readily attached. In this work we chose GFP as a scaffold and engineered many alternative oligomeric forms, driven by either specific disulfide bond formation or metal ion addition. We generated a wide range of spatial arrangements of GFP subunits from 11 different oligomeric variants, and determined their X-ray structures in a total of 33 distinct crystal forms. Some of the oligomeric GFP variants show geometric polymorphism depending on conditions, while others show considerable geometric rigidity. Potential future applications of this system are discussed.
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A Suite of Engineered GFP Molecules for Oligomeric Scaffolding.,Leibly DJ, Arbing MA, Pashkov I, DeVore N, Waldo GS, Terwilliger TC, Yeates TO Structure. 2015 Sep 1;23(9):1754-68. doi: 10.1016/j.str.2015.07.008. Epub 2015, Aug 13. PMID:26278175<ref>PMID:26278175</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4w7c" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Leibly, D J]]
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[[Category: Large Structures]]
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[[Category: Waldo, G S]]
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[[Category: Synthetic construct]]
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[[Category: Yeates, T O]]
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[[Category: Leibly DJ]]
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[[Category: Fluorescent protein]]
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[[Category: Waldo GS]]
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[[Category: Yeates TO]]

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Crystal Structure of Full-Length Split GFP Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, C 2 Space Group

PDB ID 4w7c

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