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==THE SOLUTION STRUCTURE OF A LEUCINE-ZIPPER MOTIF PEPTIDE==
==THE SOLUTION STRUCTURE OF A LEUCINE-ZIPPER MOTIF PEPTIDE==
<StructureSection load='1zta' size='340' side='right' caption='[[1zta]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1zta' size='340' side='right'caption='[[1zta]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1zta]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZTA FirstGlance]. <br>
<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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zta OCA], [http://pdbe.org/1zta PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zta RCSB], [http://www.ebi.ac.uk/pdbsum/1zta PDBsum]</span></td></tr>
</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>
</table>
== Function ==
== Function ==
[[http://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'.  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zt/1zta_consurf.spt"</scriptWhenChecked>
     <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>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Frank, R]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Gausepohl, H]]
[[Category: Castiglione Morelli MA]]
[[Category: Gibson, T]]
[[Category: Frank R]]
[[Category: Morelli, M A.Castiglione]]
[[Category: Gausepohl H]]
[[Category: Pastore, A]]
[[Category: Gibson T]]
[[Category: Saudek, V]]
[[Category: Pastore A]]
[[Category: Dna-binding motif]]
[[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

1zta is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Saudek V, Pastore A, Morelli MA, Frank R, Gausepohl H, Gibson T. The solution structure of a leucine-zipper motif peptide. Protein Eng. 1991 Jun;4(5):519-29. PMID:1891459
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