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[[Image:2b22.gif|left|200px]]
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{{STRUCTURE_2b22|  PDB=2b22  |  SCENE=  }}
'''Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat'''


==Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat==
<StructureSection load='2b22' size='340' side='right'caption='[[2b22]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2b22]] is a 1 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=2B22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B22 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]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=2b22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b22 OCA], [https://pdbe.org/2b22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b22 RCSB], [https://www.ebi.ac.uk/pdbsum/2b22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b22 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 ==
Coiled-coil sequences in proteins commonly share a seven-amino acid repeat with nonpolar side chains at the first (a) and fourth (d) positions. We investigate here the role of a 3-3-1 hydrophobic repeat containing nonpolar amino acids at the a, d, and g positions in determining the structures of coiled coils using mutants of the GCN4 leucine zipper dimerization domain. When three charged residues at the g positions in the parental sequence are replaced by nonpolar alanine or valine side chains, stable four-helix structures result. The X-ray crystal structures of the tetramers reveal antiparallel, four-stranded coiled coils in which the a, d, and g side chains interlock in a combination of knobs-into-knobs and knobs-into-holes packing. Interfacial interactions in a coiled coil can therefore be prescribed by hydrophobic-polar patterns beyond the canonical 3-4 heptad repeat. The results suggest that the conserved, charged residues at the g positions in the GCN4 leucine zipper can impart a negative design element to disfavor thermodynamically more stable, antiparallel tetramers.


==Overview==
Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat.,Deng Y, Liu J, Zheng Q, Eliezer D, Kallenbach NR, Lu M Structure. 2006 Feb;14(2):247-55. PMID:16472744<ref>PMID:16472744</ref>
Coiled-coil sequences in proteins commonly share a seven-amino acid repeat with nonpolar side chains at the first (a) and fourth (d) positions. We investigate here the role of a 3-3-1 hydrophobic repeat containing nonpolar amino acids at the a, d, and g positions in determining the structures of coiled coils using mutants of the GCN4 leucine zipper dimerization domain. When three charged residues at the g positions in the parental sequence are replaced by nonpolar alanine or valine side chains, stable four-helix structures result. The X-ray crystal structures of the tetramers reveal antiparallel, four-stranded coiled coils in which the a, d, and g side chains interlock in a combination of knobs-into-knobs and knobs-into-holes packing. Interfacial interactions in a coiled coil can therefore be prescribed by hydrophobic-polar patterns beyond the canonical 3-4 heptad repeat. The results suggest that the conserved, charged residues at the g positions in the GCN4 leucine zipper can impart a negative design element to disfavor thermodynamically more stable, antiparallel tetramers.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2B22 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=2B22 OCA].
</div>
<div class="pdbe-citations 2b22" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat., Deng Y, Liu J, Zheng Q, Eliezer D, Kallenbach NR, Lu M, Structure. 2006 Feb;14(2):247-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16472744 16472744]
*[[Gcn4 3D Structures|Gcn4 3D Structures]]
*[[Gnc4 3D Structures|Gnc4 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Deng Y]]
[[Category: Deng, Y.]]
[[Category: Eliezer D]]
[[Category: Eliezer, D.]]
[[Category: Kallenbach NR]]
[[Category: Kallenbach, N R.]]
[[Category: Liu J]]
[[Category: Liu, J.]]
[[Category: Lu M]]
[[Category: Lu, M.]]
[[Category: Zheng Q]]
[[Category: Zheng, Q.]]
[[Category: Ala coil]]
[[Category: Antiparallel tetramer]]
[[Category: Coiled coil]]
[[Category: Protein design]]
[[Category: Protein structure]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:45:21 2008''

Latest revision as of 13:04, 26 July 2023

Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat

2b22, resolution 2.00Å

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