4dme: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dme]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DME FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dme]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DME FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4dme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dme OCA], [https://pdbe.org/4dme PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dme RCSB], [https://www.ebi.ac.uk/pdbsum/4dme PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dme ProSAT]</span></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=4dme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dme OCA], [https://pdbe.org/4dme PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dme RCSB], [https://www.ebi.ac.uk/pdbsum/4dme PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dme ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The dimerization domain of the yeast transcription factor GCN4, one of the first coiled-coil proteins to be structurally characterized at high resolution, has served as the basis for numerous fundamental studies on alpha-helical folding. Mutations in the GCN4 leucine zipper are known to change its preferred oligomerization state from dimeric to trimeric or tetrameric; however, the wild-type sequence has been assumed to encode a two-chain assembly exclusively. Here we demonstrate that the GCN4 coiled-coil domain can populate either a dimer or trimer fold, depending on environment. We report high-resolution crystal structures of the wild-type sequence in dimeric and trimeric assemblies. Biophysical measurements suggest populations of both oligomerization states under certain experimental conditions in solution. We use parallel tempering molecular dynamics simulations on the microsecond timescale to compare the stability of the dimer and trimer folded states in isolation, leading to the most extensive set of simulations on the leucine zipper published to date. In total, our results suggest that the folding behavior of the well-studied GCN4 leucine-zipper domain is more complex than was previously appreciated. Our results have implications in ongoing efforts to establish predictive algorithms for coiled-coil folds and the selection of coiled-coil model systems for design and mutational studies where oligomerization state specificity is an important consideration.
The Native GCN4 Leucine-Zipper Domain Does Not Uniquely Specify a Dimeric Oligomerization State.,Oshaben KM, Salari R, McCaslin DR, Chong LT, Horne WS Biochemistry. 2012 Nov 1. PMID:23116373<ref>PMID:23116373</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4dme" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Gcn4 3D Structures|Gcn4 3D Structures]]
*[[Gnc4 3D Structures|Gnc4 3D Structures]]
*[[Gnc4 3D Structures|Gnc4 3D Structures]]
== References ==
<references/>
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__TOC__
</StructureSection>
</StructureSection>

Revision as of 14:39, 14 March 2024

GCN4 leucine zipper domain in a trimeric oligomerization state

4dme, resolution 2.20Å

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