1qtg
From Proteopedia
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| - | [[Image:1qtg.gif|left|200px]] | ||
| - | + | ==AVERAGED NMR MODEL OF SWITCH ARC, A DOUBLE MUTANT OF ARC REPRESSOR== | |
| - | + | <StructureSection load='1qtg' size='340' side='right'caption='[[1qtg]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1qtg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_virus_P22 Salmonella virus P22]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QTG FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1qtg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qtg OCA], [https://pdbe.org/1qtg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qtg RCSB], [https://www.ebi.ac.uk/pdbsum/1qtg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qtg ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | | | + | [https://www.uniprot.org/uniprot/RARC_BPP22 RARC_BPP22] This protein acts as a transcriptional repressor of its own gene arc and of gene ant. |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | + | == Publication Abstract from PubMed == | |
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A "switch" mutant of the Arc repressor homodimer was constructed by interchanging the sequence positions of a hydrophobic core residue, leucine 12, and an adjacent surface polar residue, asparagine 11, in each strand of an intersubunit beta sheet. The mutant protein adopts a fold in which each beta strand is replaced by a right-handed helix and side chains in this region undergo significant repacking. The observed structural changes allow the protein to maintain solvent exposure of polar side chains and optimal burial of hydrophobic side chains. These results suggest that new protein folds can evolve from existing folds without drastic or large-scale mutagenesis. | A "switch" mutant of the Arc repressor homodimer was constructed by interchanging the sequence positions of a hydrophobic core residue, leucine 12, and an adjacent surface polar residue, asparagine 11, in each strand of an intersubunit beta sheet. The mutant protein adopts a fold in which each beta strand is replaced by a right-handed helix and side chains in this region undergo significant repacking. The observed structural changes allow the protein to maintain solvent exposure of polar side chains and optimal burial of hydrophobic side chains. These results suggest that new protein folds can evolve from existing folds without drastic or large-scale mutagenesis. | ||
| - | + | Evolution of a protein fold in vitro.,Cordes MH, Walsh NP, McKnight CJ, Sauer RT Science. 1999 Apr 9;284(5412):325-8. PMID:10195898<ref>PMID:10195898</ref> | |
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| - | Evolution of a protein fold in vitro., Cordes MH, Walsh NP, McKnight CJ, Sauer RT | + | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 1qtg" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Salmonella virus P22]] | ||
| + | [[Category: Cordes MHJ]] | ||
| + | [[Category: McKnight CJ]] | ||
| + | [[Category: Sauer RT]] | ||
| + | [[Category: Walsh NP]] | ||
Current revision
AVERAGED NMR MODEL OF SWITCH ARC, A DOUBLE MUTANT OF ARC REPRESSOR
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