9yvx: Difference between revisions
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==Crystal structure of red fluorescent protein mRouge, 277 K== | |||
<StructureSection load='9yvx' size='340' side='right'caption='[[9yvx]], [[Resolution|resolution]] 1.38Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9yvx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Discosoma_sp. Discosoma sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9YVX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9YVX FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.38Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NRQ:{(4Z)-4-(4-HYDROXYBENZYLIDENE)-2-[3-(METHYLTHIO)PROPANIMIDOYL]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>NRQ</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=9yvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9yvx OCA], [https://pdbe.org/9yvx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9yvx RCSB], [https://www.ebi.ac.uk/pdbsum/9yvx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9yvx ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Structural dynamics play a crucial role in protein function, and tuning these dynamics through mutagenesis has emerged as a promising strategy for enhancing activity. However, identifying dynamics hotspots for protein engineering remains a labor-intensive challenge. Here, we demonstrate that NMR peak intensity analysis-a rapid, qualitative method with residue-level resolution-can identify functionally relevant dynamic regions with high precision. Using a family of red fluorescent proteins (RFPs) as a case study, we reveal that flexibility in specific regions of their structures correlates with function. Specifically, as quantum yield increases, the side of the beta-barrel closest to the chromophore phenolate moiety becomes more rigid, while the opposite side, closest to the acylimine group, gains flexibility. Notably, the phenolate face corresponds to a mutational hotspot frequently targeted in directed evolution campaigns aimed at enhancing brightness, underscoring its functional significance. B-factor analysis of non-cryogenic X-ray crystal structures further supports our findings. Our results establish NMR peak intensity analysis as a promising tool for mapping functional dynamics hotspots to guide protein engineering campaigns. | |||
Mapping functional dynamics hotspots for protein engineering with NMR peak intensity analysis.,Damry AM, Hunt SE, Legault S, Thompson MC, Goto NK, Chica RA Protein Eng Des Sel. 2026 Jan 9;39:gzag014. doi: 10.1093/protein/gzag014. PMID:42402021<ref>PMID:42402021</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 9yvx" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Discosoma sp]] | ||
[[Category: Large Structures]] | |||
[[Category: Chica RA]] | |||
[[Category: Damry AM]] | |||
[[Category: Goto NK]] | |||
[[Category: Hunt SE]] | |||
[[Category: Legault S]] | |||
[[Category: Thompson MC]] | |||
