1zij

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(New page: 200px<br /><applet load="1zij" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zij, resolution 2.00&Aring;" /> '''GCN4-LEUCINE ZIPPER ...)
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[[Image:1zij.gif|left|200px]]<br /><applet load="1zij" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zij.gif|left|200px]]<br /><applet load="1zij" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1zij, resolution 2.00&Aring;" />
caption="1zij, resolution 2.00&Aring;" />
'''GCN4-LEUCINE ZIPPER CORE MUTANT ASN16ABA IN THE TRIMERIC STATE'''<br />
'''GCN4-LEUCINE ZIPPER CORE MUTANT ASN16ABA IN THE TRIMERIC STATE'''<br />
==Overview==
==Overview==
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Each protein sequence generally adopts a single native fold, but the, sequence features that confer structural uniqueness are not well, understood. To define the basis for structural heterogeneity, we, determined the high resolution X-ray crystal structures of a single GCN4, leucine-zipper mutant (Asn 16 to aminobutyric acid) in both dimeric and, trimeric coiled-coil conformations. The mutant sequence is accommodated in, two distinct structures by forming similarly-shaped packing surfaces with, different sets of atoms. The trimer structure, in comparison to a, previously-characterized trimeric mutant with substitutions in eight core, residues, shows that the twist of individual helices and the helix-helix, crossing angles can vary significantly to produce the most favoured, packing arrangement.
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Each protein sequence generally adopts a single native fold, but the sequence features that confer structural uniqueness are not well understood. To define the basis for structural heterogeneity, we determined the high resolution X-ray crystal structures of a single GCN4 leucine-zipper mutant (Asn 16 to aminobutyric acid) in both dimeric and trimeric coiled-coil conformations. The mutant sequence is accommodated in two distinct structures by forming similarly-shaped packing surfaces with different sets of atoms. The trimer structure, in comparison to a previously-characterized trimeric mutant with substitutions in eight core residues, shows that the twist of individual helices and the helix-helix crossing angles can vary significantly to produce the most favoured packing arrangement.
==About this Structure==
==About this Structure==
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1ZIJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ACE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZIJ OCA].
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1ZIJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZIJ OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Alber, T.]]
[[Category: Alber, T.]]
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[[Category: Brown, R.A.]]
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[[Category: Brown, R A.]]
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[[Category: Junior, L.Gonzalez.]]
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[[Category: Junior, L Gonzalez.]]
[[Category: Richardson, D.]]
[[Category: Richardson, D.]]
[[Category: ACE]]
[[Category: ACE]]
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[[Category: transcription regulation]]
[[Category: transcription regulation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:28:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:15:52 2008''

Revision as of 14:15, 21 February 2008


1zij, resolution 2.00Å

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GCN4-LEUCINE ZIPPER CORE MUTANT ASN16ABA IN THE TRIMERIC STATE

Overview

Each protein sequence generally adopts a single native fold, but the sequence features that confer structural uniqueness are not well understood. To define the basis for structural heterogeneity, we determined the high resolution X-ray crystal structures of a single GCN4 leucine-zipper mutant (Asn 16 to aminobutyric acid) in both dimeric and trimeric coiled-coil conformations. The mutant sequence is accommodated in two distinct structures by forming similarly-shaped packing surfaces with different sets of atoms. The trimer structure, in comparison to a previously-characterized trimeric mutant with substitutions in eight core residues, shows that the twist of individual helices and the helix-helix crossing angles can vary significantly to produce the most favoured packing arrangement.

About this Structure

1ZIJ is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structures of a single coiled-coil peptide in two oligomeric states reveal the basis for structural polymorphism., Gonzalez L Jr, Brown RA, Richardson D, Alber T, Nat Struct Biol. 1996 Dec;3(12):1002-9. PMID:8946853

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