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[[Image:2ccf.gif|left|200px]]


{{Structure
==Antiparallel Configuration of pLI E20S==
|PDB= 2ccf |SIZE=350|CAPTION= <scene name='initialview01'>2ccf</scene>, resolution 1.70&Aring;
<StructureSection load='2ccf' size='340' side='right'caption='[[2ccf]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[2ccf]] 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=2CCF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CCF FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
|GENE=  
<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=2ccf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ccf OCA], [https://pdbe.org/2ccf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ccf RCSB], [https://www.ebi.ac.uk/pdbsum/2ccf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ccf 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 ==
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.


'''ANTIPARALLEL CONFIGURATION OF PLI E20S'''
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ccf" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Gcn4 3D Structures|Gcn4 3D Structures]]
 
*[[Gnc4 3D Structures|Gnc4 3D Structures]]
==About this Structure==
== References ==
2CCF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CCF OCA].
<references/>
 
__TOC__
==Reference==
</StructureSection>
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:[http://www.ncbi.nlm.nih.gov/pubmed/16584182 16584182]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Brooks 3rd CL]]
[[Category: Ghadiri, M R.]]
[[Category: Ghadiri MR]]
[[Category: III, C L.Brooks.]]
[[Category: Leman LJ]]
[[Category: Leman, L J.]]
[[Category: Price DJ]]
[[Category: Price, D J.]]
[[Category: Stout CD]]
[[Category: Stout, C D.]]
[[Category: Yadav MK]]
[[Category: Yadav, M K.]]
[[Category: activator]]
[[Category: amino-acid biosynthesis]]
[[Category: antiparallel]]
[[Category: dna-binding]]
[[Category: four helix bundle]]
[[Category: nuclear protein]]
[[Category: parallel]]
[[Category: pli]]
[[Category: transcription]]
[[Category: transcription regulation]]
 
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