1ysa: Difference between revisions

Revision as of 09:42, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

1ysa, resolution 2.90Å ()

Structural annotation:
Resources:	CATH : 1Ysac00, 1Ysad00 InterPro : Ipr011616, Ipr004827 Pfam : PF00170 SCOP : d1ysac_, d1ysad_ UniProt : P03069

Functional annotation:
Cellular component:	nucleus
Biological process:	positive regulation of gene-specific transcription involved in unfolded protein response amino acid biosynthetic process regulation of transcription, DNA-dependent transcription regulation of transcription from RNA polymerase II promoter
Molecular function:	protein dimerization activity transcription factor activity DNA binding sequence-specific DNA binding

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

THE GCN4 BASIC REGION LEUCINE ZIPPER BINDS DNA AS A DIMER OF UNINTERRUPTED ALPHA HELICES: CRYSTAL STRUCTURE OF THE PROTEIN-DNA COMPLEXTHE GCN4 BASIC REGION LEUCINE ZIPPER BINDS DNA AS A DIMER OF UNINTERRUPTED ALPHA HELICES: CRYSTAL STRUCTURE OF THE PROTEIN-DNA COMPLEX

Template:ABSTRACT PUBMED 1473154

About this StructureAbout this Structure

1YSA is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: crystal structure of the protein-DNA complex., Ellenberger TE, Brandl CJ, Struhl K, Harrison SC, Cell. 1992 Dec 24;71(7):1223-37. PMID:1473154

Page seeded by OCA on Tue Jul 29 09:42:32 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''THE GCN4 BASIC REGION LEUCINE ZIPPER BINDS DNA AS A DIMER OF UNINTERRUPTED ALPHA HELICES: CRYSTAL STRUCTURE OF THE PROTEIN-DNA COMPLEX'''
+===THE GCN4 BASIC REGION LEUCINE ZIPPER BINDS DNA AS A DIMER OF UNINTERRUPTED ALPHA HELICES: CRYSTAL STRUCTURE OF THE PROTEIN-DNA COMPLEX===
-==Overview==
+<!--
-The yeast transcriptional activator GCN4 is 1 of over 30 identified eukaryotic proteins containing the basic region leucine zipper (bZIP) DNA-binding motif. We have determined the crystal structure of the GCN4 bZIP element complexed with DNA at 2.9 A resolution. The bZIP dimer is a pair of continuous alpha helices that form a parallel coiled coil over their carboxy-terminal 30 residues and gradually diverge toward their amino termini to pass through the major groove of the DNA-binding site. The coiled-coil dimerization interface is oriented almost perpendicular to the DNA axis, giving the complex the appearance of the letter T. There are no kinks or sharp bends in either bZIP monomer. Numerous contacts to DNA bases and phosphate oxygens are made by basic region residues that are conserved in the bZIP protein family. The details of the bZIP dimer interaction with DNA can explain recognition of the AP-1 site by the GCN4 protein.
+The line below this paragraph, {{ABSTRACT_PUBMED_1473154}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 1473154 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_1473154}}
 ==About this Structure==
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 [[Category: Double helix]]
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