4dxm: Difference between revisions
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<StructureSection load='4dxm' size='340' side='right'caption='[[4dxm]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='4dxm' size='340' side='right'caption='[[4dxm]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4dxm]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4dxm]] 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=4DXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DXM FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CR8:2-[1-AMINO-2-(1H-IMIDAZOL-5-YL)ETHYL]-1-(CARBOXYMETHYL)-4-[(4-OXOCYCLOHEXA-2,5-DIEN-1-YLIDENE)METHYL]-1H-IMIDAZOL-5-OLATE'>CR8</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4dxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dxm OCA], [https://pdbe.org/4dxm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dxm RCSB], [https://www.ebi.ac.uk/pdbsum/4dxm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dxm ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</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 | [[Category: Synthetic construct]] | ||
[[Category: Fromme | [[Category: Fromme R]] | ||
[[Category: Kim | [[Category: Kim H]] | ||
[[Category: Wachter | [[Category: Wachter RM]] | ||
Revision as of 11:42, 21 September 2022
Crystal Structure of an ancestral GFP-like proteinCrystal Structure of an ancestral GFP-like protein
Structural highlights
Publication Abstract from PubMedIn 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 AlsoReferences
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