4dxi: Difference between revisions
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==Crystal Structure of an Ancestor of All Faviina Proteins== | ==Crystal Structure of an Ancestor of All Faviina Proteins== | ||
<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 [ | <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=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | ||
<tr id=' | <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='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='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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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 4dxi" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Green Fluorescent Protein|Green Fluorescent Protein]] | *[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Kim H]] | ||
[[Category: | [[Category: Wachter RM]] | ||
Latest revision as of 12:12, 15 November 2023
Crystal Structure of an Ancestor of All Faviina ProteinsCrystal Structure of an Ancestor of All Faviina Proteins
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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