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| | <StructureSection load='4dxi' size='340' side='right'caption='[[4dxi]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='4dxi' size='340' side='right'caption='[[4dxi]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4dxi]] 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=4DXI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DXI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4dxi]] 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=4DXI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DXI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dxi OCA], [https://pdbe.org/4dxi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dxi RCSB], [https://www.ebi.ac.uk/pdbsum/4dxi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dxi ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dxm|4dxm]], [[4dxn|4dxn]], [[4dxo|4dxo]], [[4dxp|4dxp]], [[4dxq|4dxq]]</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=4dxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dxi OCA], [http://pdbe.org/4dxi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dxi RCSB], [http://www.ebi.ac.uk/pdbsum/4dxi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dxi ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Green Fluorescent Protein|Green Fluorescent Protein]] | + | *[[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: Kim, H]] | + | [[Category: Kim H]] |
| - | [[Category: Wachter, R M]] | + | [[Category: Wachter RM]] |
| - | [[Category: Beta barrel]]
| + | |
| - | [[Category: Luminescent protein]]
| + | |
| Structural highlights
Publication Abstract from PubMed
In proteins, functional divergence involves mutations that modify structure and dynamics. Here we provide experimental evidence for an evolutionary mechanism driven solely by long-range dynamic motions without significant backbone adjustments, catalytic group rearrangements, or changes in subunit assembly. Crystallographic structures were determined for several reconstructed ancestral proteins belonging to a GFP class frequently employed in superresolution microscopy. Their chain flexibility was analyzed using molecular dynamics and perturbation response scanning. The green-to-red photoconvertible phenotype appears to have arisen from a common green ancestor by migration of a knob-like anchoring region away from the active site diagonally across the beta barrel fold. The allosterically coupled mutational sites provide active site conformational mobility via epistasis. We propose that light-induced chromophore twisting is enhanced in a reverse-protonated subpopulation, activating internal acid-base chemistry and backbone cleavage to enlarge the chromophore. Dynamics-driven hinge migration may represent a more general platform for the evolution of novel enzyme activities.
A hinge migration mechanism unlocks the evolution of green-to-red photoconversion in GFP-like proteins.,Kim H, Zou T, Modi C, Dorner K, Grunkemeyer TJ, Chen L, Fromme R, Matz MV, Ozkan SB, Wachter RM Structure. 2015 Jan 6;23(1):34-43. doi: 10.1016/j.str.2014.11.011. PMID:25565105[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kim H, Zou T, Modi C, Dorner K, Grunkemeyer TJ, Chen L, Fromme R, Matz MV, Ozkan SB, Wachter RM. A hinge migration mechanism unlocks the evolution of green-to-red photoconversion in GFP-like proteins. Structure. 2015 Jan 6;23(1):34-43. doi: 10.1016/j.str.2014.11.011. PMID:25565105 doi:http://dx.doi.org/10.1016/j.str.2014.11.011
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