1gd2: Difference between revisions

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[[Image:1gd2.gif|left|200px]]<br /><applet load="1gd2" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1gd2.gif|left|200px]]<br /><applet load="1gd2" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1gd2, resolution 2.0Å" />

'''CRYSTAL STRUCTURE OF BZIP TRANSCRIPTION FACTOR PAP1 BOUND TO DNA'''<br />

==Overview==

The basic region leucine zipper (bZIP) proteins form one of the largest, families of transcription factors in eukaryotic cells. Despite relatively, high homology between the amino acid sequences of the bZIP motifs, these, proteins recognize diverse DNA sequences. Here we report the 2.0 A, resolution crystal structure of the bZIP motif of one such transcription, factor, PAP1, a fission yeast AP-1-like transcription factor that binds, DNA containing the novel consensus sequence TTACGTAA. The structure, reveals how the Pap1-specific residues of the bZIP basic region recognize, the target sequence and shows that the side chain of the invariant Asn in, the bZIP motif adopts an alternative conformation in Pap1. This, conformation, which is stabilized by a Pap1-specific residue and its, associated water molecule, recognizes a different base in the target, sequence from that in other bZIP subfamilies.

The basic region leucine zipper (bZIP) proteins form one of the largest families of transcription factors in eukaryotic cells. Despite relatively high homology between the amino acid sequences of the bZIP motifs, these proteins recognize diverse DNA sequences. Here we report the 2.0 A resolution crystal structure of the bZIP motif of one such transcription factor, PAP1, a fission yeast AP-1-like transcription factor that binds DNA containing the novel consensus sequence TTACGTAA. The structure reveals how the Pap1-specific residues of the bZIP basic region recognize the target sequence and shows that the side chain of the invariant Asn in the bZIP motif adopts an alternative conformation in Pap1. This conformation, which is stabilized by a Pap1-specific residue and its associated water molecule, recognizes a different base in the target sequence from that in other bZIP subfamilies.

==About this Structure==

1GD2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1GD2 OCA].

1GD2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GD2 OCA].

==Reference==

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[[Category: protein-dna complex]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 15~~:57:~~26 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:46 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1gd2.gif|left|200px]]<br /><applet load="1gd2" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1gd2.gif|left|200px]]<br /><applet load="1gd2" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1gd2, resolution 2.0&Aring;" />
 '''CRYSTAL STRUCTURE OF BZIP TRANSCRIPTION FACTOR PAP1 BOUND TO DNA'''<br />
 ==Overview==
-The basic region leucine zipper (bZIP) proteins form one of the largest, families of transcription factors in eukaryotic cells. Despite relatively, high homology between the amino acid sequences of the bZIP motifs, these, proteins recognize diverse DNA sequences. Here we report the 2.0 A, resolution crystal structure of the bZIP motif of one such transcription, factor, PAP1, a fission yeast AP-1-like transcription factor that binds, DNA containing the novel consensus sequence TTACGTAA. The structure, reveals how the Pap1-specific residues of the bZIP basic region recognize, the target sequence and shows that the side chain of the invariant Asn in, the bZIP motif adopts an alternative conformation in Pap1. This, conformation, which is stabilized by a Pap1-specific residue and its, associated water molecule, recognizes a different base in the target, sequence from that in other bZIP subfamilies.
+The basic region leucine zipper (bZIP) proteins form one of the largest families of transcription factors in eukaryotic cells. Despite relatively high homology between the amino acid sequences of the bZIP motifs, these proteins recognize diverse DNA sequences. Here we report the 2.0 A resolution crystal structure of the bZIP motif of one such transcription factor, PAP1, a fission yeast AP-1-like transcription factor that binds DNA containing the novel consensus sequence TTACGTAA. The structure reveals how the Pap1-specific residues of the bZIP basic region recognize the target sequence and shows that the side chain of the invariant Asn in the bZIP motif adopts an alternative conformation in Pap1. This conformation, which is stabilized by a Pap1-specific residue and its associated water molecule, recognizes a different base in the target sequence from that in other bZIP subfamilies.
 ==About this Structure==
-GD2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GD2 OCA].
+GD2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GD2 OCA].
 ==Reference==
@@ Line 21: / Line 21: @@
 [[Category: protein-dna complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:57:26 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:46 2008''