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| | <StructureSection load='4tza' size='340' side='right'caption='[[4tza]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='4tza' size='340' side='right'caption='[[4tza]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4tza]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TZA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TZA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4tza]] 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=4TZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TZA FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CRQ:[2-(3-CARBAMOYL-1-IMINO-PROPYL)-4-(4-HYDROXY-BENZYLIDENE)-5-OXO-4,5-DIHYDRO-IMIDAZOL-1-YL]-ACETIC+ACID'>CRQ</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=4tza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tza OCA], [http://pdbe.org/4tza PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tza RCSB], [http://www.ebi.ac.uk/pdbsum/4tza PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tza ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRQ:[2-(3-CARBAMOYL-1-IMINO-PROPYL)-4-(4-HYDROXY-BENZYLIDENE)-5-OXO-4,5-DIHYDRO-IMIDAZOL-1-YL]-ACETIC+ACID'>CRQ</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=4tza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tza OCA], [https://pdbe.org/4tza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tza RCSB], [https://www.ebi.ac.uk/pdbsum/4tza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tza ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4tza" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4tza" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Synthetic construct sequences]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Bradbury, A R.M]] | + | [[Category: Bradbury ARM]] |
| - | [[Category: Close, D W]] | + | [[Category: Close DW]] |
| - | [[Category: Engineered]]
| + | |
| - | [[Category: Fluorescent protein]]
| + | |
| - | [[Category: Thermostable]]
| + | |
| Structural highlights
Publication Abstract from PubMed
In this paper we describe the engineering and X-ray crystal structure of Thermal Green Protein (TGP), an extremely stable, highly soluble, non-aggregating green fluorescent protein. TGP is a soluble variant of the fluorescent protein eCGP123, which despite being highly stable, has proven to be aggregation-prone. The X-ray crystal structure of eCGP123, also determined within the context of this paper, was used to carry out rational surface engineering to improve its solubility, leading to TGP. The approach involved simultaneously eliminating crystal lattice contacts while increasing the overall negative charge of the protein. Despite intentional disruption of lattice contacts and introduction of high entropy glutamate side chains, TGP crystallized readily in a number of different conditions and the X-ray crystal structure of TGP was determined to 1.9 A resolution. The structural reasons for the enhanced stability of TGP and eCGP123 are discussed. We demonstrate the utility of using TGP as a fusion partner in various assays and significantly, in amyloid assays in which the standard fluorescent protein, EGFP, is undesirable because of aberrant oligomerization. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc.
TGP, an extremely stable, non-aggregating fluorescent protein created by structure-guided surface engineering.,Close DW, Don Paul C, Langan PS, Wilce MC, Traore DA, Halfmann R, Rocha RC, Waldo GS, Payne RJ, Rucker JB, Prescott M, Bradbury AR Proteins. 2014 Oct 7. doi: 10.1002/prot.24699. PMID:25287913[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Close DW, Don Paul C, Langan PS, Wilce MC, Traore DA, Halfmann R, Rocha RC, Waldo GS, Payne RJ, Rucker JB, Prescott M, Bradbury AR. TGP, an extremely stable, non-aggregating fluorescent protein created by structure-guided surface engineering. Proteins. 2014 Oct 7. doi: 10.1002/prot.24699. PMID:25287913 doi:http://dx.doi.org/10.1002/prot.24699
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