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2ccn

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<StructureSection load='2ccn' size='340' side='right'caption='[[2ccn]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='2ccn' size='340' side='right'caption='[[2ccn]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2ccn]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vzl 1vzl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CCN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2ccn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vzl 1vzl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CCN FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ce9|1ce9]], [[1dgc|1dgc]], [[1env|1env]], [[1fav|1fav]], [[1gcl|1gcl]], [[1gcm|1gcm]], [[1gk6|1gk6]], [[1gzl|1gzl]], [[1ihq|1ihq]], [[1ij0|1ij0]], [[1ij1|1ij1]], [[1ij2|1ij2]], [[1ij3|1ij3]], [[1kql|1kql]], [[1ld4|1ld4]], [[1llm|1llm]], [[1nkn|1nkn]], [[1piq|1piq]], [[1rb1|1rb1]], [[1rb4|1rb4]], [[1rb5|1rb5]], [[1rb6|1rb6]], [[1swi|1swi]], [[1tmz|1tmz]], [[1unt|1unt]], [[1unu|1unu]], [[1unv|1unv]], [[1unw|1unw]], [[1unx|1unx]], [[1uny|1uny]], [[1unz|1unz]], [[1uo0|1uo0]], [[1uo1|1uo1]], [[1uo2|1uo2]], [[1uo3|1uo3]], [[1uo4|1uo4]], [[1uo5|1uo5]], [[1vzl|1vzl]], [[1w5g|1w5g]], [[1w5h|1w5h]], [[1w5i|1w5i]], [[1w5j|1w5j]], [[1w5k|1w5k]], [[1w5l|1w5l]], [[1ysa|1ysa]], [[1zii|1zii]], [[1zij|1zij]], [[1zik|1zik]], [[1zil|1zil]], [[1zim|1zim]], [[1zta|1zta]], [[2bni|2bni]], [[2cce|2cce]], [[2ccf|2ccf]], [[2dgc|2dgc]], [[2zta|2zta]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</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=2ccn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ccn OCA], [https://pdbe.org/2ccn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ccn RCSB], [https://www.ebi.ac.uk/pdbsum/2ccn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ccn 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=2ccn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ccn OCA], [https://pdbe.org/2ccn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ccn RCSB], [https://www.ebi.ac.uk/pdbsum/2ccn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ccn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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'.
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[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'.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A detailed understanding of the mechanisms by which particular amino acid sequences can give rise to more than one folded structure, such as for proteins that undergo large conformational changes or misfolding, is a long-standing objective of protein chemistry. Here, we describe the crystal structures of a single coiled-coil peptide in distinct parallel and antiparallel tetrameric configurations and further describe the parallel or antiparallel crystal structures of several related peptide sequences; the antiparallel tetrameric assemblies represent the first crystal structures of GCN4-derived peptides exhibiting such a configuration. Intriguingly, substitution of a single solvent-exposed residue enabled the parallel coiled-coil tetramer GCN4-pLI to populate the antiparallel configuration, suggesting that the two configurations are close enough in energy for subtle sequence changes to have important structural consequences. We present a structural analysis of the small changes to the helix register and side-chain conformations that accommodate the two configurations and have supplemented these results using solution studies and a molecular dynamics energetic analysis using a replica exchange methodology. Considering the previous examples of structural nonspecificity in coiled-coil peptides, the findings reported here not only emphasize the predisposition of the coiled-coil motif to adopt multiple configurations but also call attention to the associated risk that observed crytstal structures may not represent the only (or even the major) species present in solution.
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Coiled coils at the edge of configurational heterogeneity. Structural analyses of parallel and antiparallel homotetrameric coiled coils reveal configurational sensitivity to a single solvent-exposed amino acid substitution.,Yadav MK, Leman LJ, Price DJ, Brooks CL 3rd, Stout CD, Ghadiri MR Biochemistry. 2006 Apr 11;45(14):4463-73. PMID:16584182<ref>PMID:16584182</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2ccn" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Gcn4 3D Structures|Gcn4 3D Structures]]
*[[Gnc4 3D Structures|Gnc4 3D Structures]]
*[[Gnc4 3D Structures|Gnc4 3D Structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: 3rd, C L.Brooks]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Ghadiri, M R]]
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[[Category: Brooks 3rd CL]]
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[[Category: Leman, L J]]
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[[Category: Ghadiri MR]]
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[[Category: Price, D J]]
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[[Category: Leman LJ]]
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[[Category: Stout, C D]]
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[[Category: Price DJ]]
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[[Category: Yadav, M K]]
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[[Category: Stout CD]]
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[[Category: Activator]]
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[[Category: Yadav MK]]
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[[Category: Amino-acid biosynthesis]]
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[[Category: Antiparallel]]
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[[Category: Dna-binding]]
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[[Category: Four helix bundle]]
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[[Category: Nuclear protein]]
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[[Category: Parallel]]
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[[Category: Pli]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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Revision as of 11:15, 21 February 2024

pLI E20C is antiparallel

PDB ID 2ccn

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