1ce9

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[[Image:1ce9.jpg|left|200px]]
 
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==HELIX CAPPING IN THE GCN4 LEUCINE ZIPPER==
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The line below this paragraph, containing "STRUCTURE_1ce9", creates the "Structure Box" on the page.
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<StructureSection load='1ce9' size='340' side='right'caption='[[1ce9]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ce9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CE9 FirstGlance]. <br>
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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]] 1.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ce9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ce9 OCA], [https://pdbe.org/1ce9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ce9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ce9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ce9 ProSAT]</span></td></tr>
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{{STRUCTURE_1ce9| PDB=1ce9 | SCENE= }}
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</table>
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== 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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Capping interactions associated with specific sequences at or near the ends of alpha-helices are important determinants of the stability of protein secondary and tertiary structure. We investigate here the role of the helix-capping motif Ser-X-X-Glu, a sequence that occurs frequently at the N termini of alpha helices in proteins, on the conformation and stability of the GCN4 leucine zipper. The 1.8 A resolution crystal structure of the capped molecule reveals distinct conformations, packing geometries and hydrogen-bonding networks at the amino terminus of the two helices in the leucine zipper dimer. The free energy of helix stabilization associated with the hydrogen-bonding and hydrophobic interactions in this capping structure is -1.2 kcal/mol, evaluated from thermal unfolding experiments. A single cap thus contributes appreciably to stabilizing the terminated helix and thereby the native state. These results suggest that helix capping plays a further role in protein folding, providing a sensitive connector linking alpha-helix formation to the developing tertiary structure of a protein.
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'''HELIX CAPPING IN THE GCN4 LEUCINE ZIPPER'''
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Helix capping in the GCN4 leucine zipper.,Lu M, Shu W, Ji H, Spek E, Wang L, Kallenbach NR J Mol Biol. 1999 May 14;288(4):743-52. PMID:10329176<ref>PMID:10329176</ref>
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==Overview==
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Capping interactions associated with specific sequences at or near the ends of alpha-helices are important determinants of the stability of protein secondary and tertiary structure. We investigate here the role of the helix-capping motif Ser-X-X-Glu, a sequence that occurs frequently at the N termini of alpha helices in proteins, on the conformation and stability of the GCN4 leucine zipper. The 1.8 A resolution crystal structure of the capped molecule reveals distinct conformations, packing geometries and hydrogen-bonding networks at the amino terminus of the two helices in the leucine zipper dimer. The free energy of helix stabilization associated with the hydrogen-bonding and hydrophobic interactions in this capping structure is -1.2 kcal/mol, evaluated from thermal unfolding experiments. A single cap thus contributes appreciably to stabilizing the terminated helix and thereby the native state. These results suggest that helix capping plays a further role in protein folding, providing a sensitive connector linking alpha-helix formation to the developing tertiary structure of a protein.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1CE9 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CE9 OCA].
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</div>
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<div class="pdbe-citations 1ce9" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Helix capping in the GCN4 leucine zipper., Lu M, Shu W, Ji H, Spek E, Wang L, Kallenbach NR, J Mol Biol. 1999 May 14;288(4):743-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10329176 10329176]
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*[[Gcn4 3D Structures|Gcn4 3D Structures]]
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[[Category: Single protein]]
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*[[Gnc4 3D Structures|Gnc4 3D Structures]]
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[[Category: Ji, H.]]
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== References ==
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[[Category: Kallenbach, N R.]]
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<references/>
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[[Category: Lu, M.]]
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__TOC__
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[[Category: Shu, W.]]
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</StructureSection>
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[[Category: Spek, E.]]
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[[Category: Large Structures]]
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[[Category: Wang, L Y.]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Coiled coil]]
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[[Category: Ji H]]
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[[Category: Helix capping]]
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[[Category: Kallenbach NR]]
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[[Category: Hydrogen bonding]]
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[[Category: Lu M]]
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[[Category: Leucine zipper]]
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[[Category: Shu W]]
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[[Category: Protein folding]]
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[[Category: Spek E]]
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[[Category: Thermal stability]]
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[[Category: Wang L-Y]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:37:58 2008''
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HELIX CAPPING IN THE GCN4 LEUCINE ZIPPER

PDB ID 1ce9

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