1gcl: Difference between revisions

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-[[Image:1gcl.jpg|left|200px]]
- {{Structure
+==GCN4 LEUCINE ZIPPER CORE MUTANT P-LI==
-|PDB= 1gcl |SIZE=350|CAPTION= <scene name='initialview01'>1gcl</scene>, resolution 2.1&Aring;
+<StructureSection load='1gcl' size='340' side='right'caption='[[1gcl]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene>
+<table><tr><td colspan='2'>[[1gcl]] is a 4 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=1GCL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GCL 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]] 2.1&#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=1gcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gcl OCA], [https://pdbe.org/1gcl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gcl RCSB], [https://www.ebi.ac.uk/pdbsum/1gcl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gcl 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 consist of heptad repeats containing two characteristic hydrophobic positions. The role of these buried hydrophobic residues in determining the structures of coiled coils was investigated by studying mutants of the GCN4 leucine zipper. When sets of buried residues were altered, two-, three-, and four-helix structures were formed. The x-ray crystal structure of the tetramer revealed a parallel, four-stranded coiled coil. In the tetramer conformation, the local packing geometry of the two hydrophobic positions in the heptad repeat is reversed relative to that in the dimer. These studies demonstrate that conserved, buried residues in the GCN4 leucine zipper direct dimer formation. In contrast to proposals that the pattern of hydrophobic and polar amino acids in a protein sequence is sufficient to determine three-dimensional structure, the shapes of buried side chains in coiled coils are essential determinants of the global fold.
-'''GCN4 LEUCINE ZIPPER CORE MUTANT P-LI'''
+A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants.,Harbury PB, Zhang T, Kim PS, Alber T Science. 1993 Nov 26;262(5138):1401-7. PMID:8248779<ref>PMID:8248779</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1gcl" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-Coiled-coil sequences in proteins consist of heptad repeats containing two characteristic hydrophobic positions. The role of these buried hydrophobic residues in determining the structures of coiled coils was investigated by studying mutants of the GCN4 leucine zipper. When sets of buried residues were altered, two-, three-, and four-helix structures were formed. The x-ray crystal structure of the tetramer revealed a parallel, four-stranded coiled coil. In the tetramer conformation, the local packing geometry of the two hydrophobic positions in the heptad repeat is reversed relative to that in the dimer. These studies demonstrate that conserved, buried residues in the GCN4 leucine zipper direct dimer formation. In contrast to proposals that the pattern of hydrophobic and polar amino acids in a protein sequence is sufficient to determine three-dimensional structure, the shapes of buried side chains in coiled coils are essential determinants of the global fold.
+*[[Gcn4 3D Structures|Gcn4 3D Structures]]
+*[[Gnc4 3D Structures|Gnc4 3D Structures]]
-==About this Structure==
+== References ==
-GCL 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=1GCL OCA].
+<references/>
+__TOC__
-==Reference==
+</StructureSection>
-A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants., Harbury PB, Zhang T, Kim PS, Alber T, Science. 1993 Nov 26;262(5138):1401-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8248779 8248779]
+[[Category: Large Structures]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Single protein]]
+[[Category: Alber T]]
-[[Category: Alber, T.]]
+[[Category: Harbury PB]]
-[[Category: Harbury, P B.]]
+[[Category: Kim PS]]
-[[Category: Kim, P S.]]
+[[Category: Zhang T]]
-[[Category: Zhang, T.]]
-[[Category: ACE]]
-[[Category: hydrophobic core mutant]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:21:20 2008''