1zta: Difference between revisions
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==THE SOLUTION STRUCTURE OF A LEUCINE-ZIPPER MOTIF PEPTIDE== | |||
<StructureSection load='1zta' size='340' side='right'caption='[[1zta]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1zta]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZTA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZTA FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1zta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zta OCA], [https://pdbe.org/1zta PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zta RCSB], [https://www.ebi.ac.uk/pdbsum/1zta PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zta 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'. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zt/1zta_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zta ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We report the complete structure determination of a 34 residue synthetic peptide with the amino acid sequence of the dimerization domain (leucine zipper) of GCN4. A high resolution structure in solution was obtained by 1H-NMR studies and distance geometry calculations followed by restrained energy minimization. A set of 20 final structures was obtained with an average root mean square deviation of 1.3 A for the backbone atoms (excluding the first and the last two residues). The structure contains an uninterrupted helix. A comparison with a structure previously determined for a larger peptide containing both the DNA-binding region (basic region) and the leucine-zipper motif shows the structural independence of the leucine-zipper domain from the contiguous DNA binding region. | |||
The solution structure of a leucine-zipper motif peptide.,Saudek V, Pastore A, Morelli MA, Frank R, Gausepohl H, Gibson T Protein Eng. 1991 Jun;4(5):519-29. PMID:1891459<ref>PMID:1891459</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1zta" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: | [[Category: Castiglione Morelli MA]] | ||
[[Category: | [[Category: Frank R]] | ||
[[Category: | [[Category: Gausepohl H]] | ||
[[Category: | [[Category: Gibson T]] | ||
[[Category: Pastore | [[Category: Pastore A]] | ||
[[Category: Saudek | [[Category: Saudek V]] | ||
Latest revision as of 11:12, 15 May 2024
THE SOLUTION STRUCTURE OF A LEUCINE-ZIPPER MOTIF PEPTIDETHE SOLUTION STRUCTURE OF A LEUCINE-ZIPPER MOTIF PEPTIDE
Structural highlights
FunctionGCN4_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'. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe report the complete structure determination of a 34 residue synthetic peptide with the amino acid sequence of the dimerization domain (leucine zipper) of GCN4. A high resolution structure in solution was obtained by 1H-NMR studies and distance geometry calculations followed by restrained energy minimization. A set of 20 final structures was obtained with an average root mean square deviation of 1.3 A for the backbone atoms (excluding the first and the last two residues). The structure contains an uninterrupted helix. A comparison with a structure previously determined for a larger peptide containing both the DNA-binding region (basic region) and the leucine-zipper motif shows the structural independence of the leucine-zipper domain from the contiguous DNA binding region. The solution structure of a leucine-zipper motif peptide.,Saudek V, Pastore A, Morelli MA, Frank R, Gausepohl H, Gibson T Protein Eng. 1991 Jun;4(5):519-29. PMID:1891459[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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