9z1v: Difference between revisions
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==Backbone Modification in the GCN4 Leucine Zipper: Calpha-methyl-Lys at position 28== | |||
<StructureSection load='9z1v' size='340' side='right'caption='[[9z1v]], [[Resolution|resolution]] 1.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9z1v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9Z1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9Z1V 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]] 1.65Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1BEB:(2~{S})-2,6-bis(azanyl)-2-methyl-hexanoic+acid'>A1BEB</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=9z1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9z1v OCA], [https://pdbe.org/9z1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9z1v RCSB], [https://www.ebi.ac.uk/pdbsum/9z1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9z1v ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GCN4_YEAST GCN4_YEAST] Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein unfolded states are heterogeneous but can manifest local and long-range order. Replacement of side chains through site-directed mutagenesis is a common method to manipulate the unfolded state and elucidate its role in the folding process. Modification of the protein backbone represents a less explored complementary approach with the potential to elicit dramatic changes in conformational preferences from minimal chemical alteration. Prior work has shown backbone modification can affect unfolded ensembles as well as intrinsically disordered sequences. Here, we show that it can be used to rationally tune structural characteristics of the unfolded state of a folded protein. Using the GCN4 leucine zipper as a host, canonical alpha-residues throughout the chain are individually replaced by beta(3) or C(alpha)-Me-alpha analogues. The former modification enhances conformational freedom, the latter restricts it, and both retain the side chain at the substitution site. Characterization by circular dichroism and X-ray crystallography shows that the variants adopt folded structures identical to the prototype. Thermal and thermodynamic stability vary in complex ways with the context and nature of backbone modification; however, a uniform relationship is observed between substitution type and the sensitivity of folding free energy to chemical denaturant. This finding suggests systematic changes in solvent-accessible surface area of the unfolded ensemble among isomeric proteins differing only in the position of a single CH(2) group. Collectively, these results demonstrate a platform for predictably tuning the properties of the unfolded state through minimal chemical modification, enabling new avenues for fundamental research on folding behavior of proteins as well as protein mimetics. | |||
Manipulating the Unfolded State of a Folded Protein through Site-Specific Backbone Modification.,Page GE, Lin Y, Horne WS Biochemistry. 2026 Mar 17;65(6):693-703. doi: 10.1021/acs.biochem.5c00687. Epub , 2026 Mar 3. PMID:41773780<ref>PMID:41773780</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 9z1v" style="background-color:#fffaf0;"></div> | ||
[[Category: Lin | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae]] | |||
[[Category: Horne WS]] | |||
[[Category: Lin Y]] | |||
[[Category: Page GE]] | |||
