5yct: Difference between revisions
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New page: '''Unreleased structure''' The entry 5yct is ON HOLD until Paper Publication Authors: Surana, P., Nandwani, N., Udgaonkar, J.B., Gosavi, S., Das, R. Description: Engineered hairpin loo... |
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==Engineered hairpin loop3 mutant monomer in Single-chain Monellin== | |||
<StructureSection load='5yct' size='340' side='right'caption='[[5yct]], [[Resolution|resolution]] 1.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5yct]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dioscoreophyllum_cumminsii Dioscoreophyllum cumminsii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YCT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YCT 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]] 1.851Å</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=5yct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yct OCA], [https://pdbe.org/5yct PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yct RCSB], [https://www.ebi.ac.uk/pdbsum/5yct PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yct ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MONA_DIOCU MONA_DIOCU] Taste-modifying protein; intensely sweet-tasting protein.[https://www.uniprot.org/uniprot/MONB_DIOCU MONB_DIOCU] Taste-modifying protein; intensely sweet-tasting protein. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Domain swapping is the process by which identical monomeric proteins exchange structural elements to generate dimers/oligomers. Although engineered domain swapping is a compelling strategy for protein assembly, its application has been limited due to the lack of simple and reliable design approaches. Here, we demonstrate that the hydrophobic five-residue 'cystatin motif' (QVVAG) from the domain-swapping protein Stefin B, when engineered into a solvent-exposed, tight surface loop between two beta-strands prevents the loop from folding back upon itself, and drives domain swapping in non-domain-swapping proteins. High-resolution structural studies demonstrate that engineering the QVVAG stretch independently into various surface loops of four structurally distinct non-domain-swapping proteins enabled the design of different modes of domain swapping in these proteins, including single, double and open-ended domain swapping. These results suggest that the introduction of the QVVAG motif can be used as a mutational approach for engineering domain swapping in diverse beta-hairpin proteins. | |||
A five-residue motif for the design of domain swapping in proteins.,Nandwani N, Surana P, Negi H, Mascarenhas NM, Udgaonkar JB, Das R, Gosavi S Nat Commun. 2019 Jan 28;10(1):452. doi: 10.1038/s41467-019-08295-x. PMID:30692525<ref>PMID:30692525</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5yct" style="background-color:#fffaf0;"></div> | ||
[[Category: Das | == References == | ||
[[Category: | <references/> | ||
[[Category: Nandwani | __TOC__ | ||
[[Category: Surana | </StructureSection> | ||
[[Category: Dioscoreophyllum cumminsii]] | |||
[[Category: Large Structures]] | |||
[[Category: Das R]] | |||
[[Category: Gosavi S]] | |||
[[Category: Nandwani N]] | |||
[[Category: Surana P]] | |||
[[Category: Udgaonkar JB]] | |||
