2ovn

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(New page: 200px<br /><applet load="2ovn" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ovn" /> '''NMR structure of the GCN4 trigger peptide'''...)
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[[Image:2ovn.jpg|left|200px]]<br /><applet load="2ovn" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ovn" />
 
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'''NMR structure of the GCN4 trigger peptide'''<br />
 
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==Overview==
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==NMR structure of the GCN4 trigger peptide==
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Coiled coils have attracted considerable interest as design templates in a, wide range of applications. Successful coiled-coil design strategies, therefore require a detailed understanding of coiled-coil folding. One, common feature shared by coiled coils is the presence of a short, autonomous helical folding unit, termed "trigger sequence," that is, indispensable for folding. Detailed knowledge of trigger sequences at the, molecular level is thus key to a general understanding of coiled-coil, formation. Using a multidisciplinary approach, we identify and, characterize here the molecular determinants that specify the helical, conformation of the monomeric early folding intermediate of the GCN4, coiled coil. We demonstrate that a network of hydrogen-bonding and, electrostatic interactions stabilize the trigger-sequence helix. This, network is rearranged in the final dimeric coiled-coil structure, and its, destabilization significantly slows down GCN4 leucine zipper folding. Our, findings provide a general explanation for the molecular mechanism of, coiled-coil formation.
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<StructureSection load='2ovn' size='340' side='right'caption='[[2ovn]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2ovn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OVN 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">Solution NMR</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=2ovn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ovn OCA], [https://pdbe.org/2ovn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ovn RCSB], [https://www.ebi.ac.uk/pdbsum/2ovn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ovn ProSAT]</span></td></tr>
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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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Coiled coils have attracted considerable interest as design templates in a wide range of applications. Successful coiled-coil design strategies therefore require a detailed understanding of coiled-coil folding. One common feature shared by coiled coils is the presence of a short autonomous helical folding unit, termed "trigger sequence," that is indispensable for folding. Detailed knowledge of trigger sequences at the molecular level is thus key to a general understanding of coiled-coil formation. Using a multidisciplinary approach, we identify and characterize here the molecular determinants that specify the helical conformation of the monomeric early folding intermediate of the GCN4 coiled coil. We demonstrate that a network of hydrogen-bonding and electrostatic interactions stabilize the trigger-sequence helix. This network is rearranged in the final dimeric coiled-coil structure, and its destabilization significantly slows down GCN4 leucine zipper folding. Our findings provide a general explanation for the molecular mechanism of coiled-coil formation.
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==About this Structure==
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Molecular basis of coiled-coil formation.,Steinmetz MO, Jelesarov I, Matousek WM, Honnappa S, Jahnke W, Missimer JH, Frank S, Alexandrescu AT, Kammerer RA Proc Natl Acad Sci U S A. 2007 Apr 24;104(17):7062-7. Epub 2007 Apr 16. PMID:17438295<ref>PMID:17438295</ref>
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2OVN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OVN OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Molecular basis of coiled-coil formation., Steinmetz MO, Jelesarov I, Matousek WM, Honnappa S, Jahnke W, Missimer JH, Frank S, Alexandrescu AT, Kammerer RA, Proc Natl Acad Sci U S A. 2007 Apr 24;104(17):7062-7. Epub 2007 Apr 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17438295 17438295]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 2ovn" style="background-color:#fffaf0;"></div>
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[[Category: Alexandrescu, A.T.]]
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[[Category: Matousek, W.M.]]
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[[Category: coiled-coil]]
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[[Category: gcn4]]
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[[Category: trigger peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:05:09 2008''
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==See Also==
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*[[Gcn4 3D Structures|Gcn4 3D Structures]]
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*[[Gnc4 3D Structures|Gnc4 3D Structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Alexandrescu AT]]
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[[Category: Matousek WM]]

Current revision

NMR structure of the GCN4 trigger peptide

PDB ID 2ovn

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