5xfu
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Domain swapped dimer crystal structure of loop1 deletion mutant in Single-chain Monellin== | |
| + | <StructureSection load='5xfu' size='340' side='right' caption='[[5xfu]], [[Resolution|resolution]] 2.61Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5xfu]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XFU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XFU FirstGlance]. <br> | ||
| + | </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=5xfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xfu OCA], [http://pdbe.org/5xfu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xfu RCSB], [http://www.ebi.ac.uk/pdbsum/5xfu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xfu ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MONB_DIOCU MONB_DIOCU]] Taste-modifying protein; intensely sweet-tasting protein. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Rational engineering of a protein to enable domain swapping requires an understanding of the sequence, structural and energetic factors that favor the domain-swapped oligomer over the monomer. While it is known that the deletion of loops between beta-strands can promote domain swapping, the spliced sequence at the position of the loop deletion is thought to have a minimal role to play in such domain swapping. Here, two loop-deletion mutants of the non-domain-swapping protein monellin, frame-shifted by a single residue, were designed. Although the spliced sequence in the two mutants differed by only one residue at the site of the deletion, only one of them (YEIKG) promoted domain swapping. The mutant containing the spliced sequence YENKG was entirely monomeric. This new understanding that the domain swapping propensity after loop deletion may depend critically on the chemical composition of the shortened loop will facilitate the rational design of domain swapping. | ||
| - | + | Amino-acid composition after loop deletion drives domain swapping.,Nandwani N, Surana P, Udgaonkar JB, Das R, Gosavi S Protein Sci. 2017 Oct;26(10):1994-2002. doi: 10.1002/pro.3237. Epub 2017 Aug 30. PMID:28710790<ref>PMID:28710790</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5xfu" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Das, R]] | ||
| + | [[Category: Gosavi, S]] | ||
| + | [[Category: Nandwani, N]] | ||
| + | [[Category: Surana, P]] | ||
| + | [[Category: Udgaonkar, J]] | ||
| + | [[Category: Domain swapped dimer]] | ||
| + | [[Category: Hinge loop composition]] | ||
| + | [[Category: Loop deletion]] | ||
| + | [[Category: Plant protein]] | ||
| + | [[Category: Single-chain monellin]] | ||
Revision as of 09:10, 4 October 2017
Domain swapped dimer crystal structure of loop1 deletion mutant in Single-chain Monellin
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