This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1zii
From Proteopedia
(New page: 200px<br /><applet load="1zii" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zii, resolution 1.8Å" /> '''GCN4-LEUCINE ZIPPER C...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1zii.gif|left|200px]]<br /><applet load="1zii" size=" | + | [[Image:1zii.gif|left|200px]]<br /><applet load="1zii" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zii, resolution 1.8Å" /> | caption="1zii, resolution 1.8Å" /> | ||
'''GCN4-LEUCINE ZIPPER CORE MUTANT ASN16ABA IN THE DIMERIC STATE'''<br /> | '''GCN4-LEUCINE ZIPPER CORE MUTANT ASN16ABA IN THE DIMERIC STATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Each protein sequence generally adopts a single native fold, but the | + | 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== | ||
| - | 1ZII 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:// | + | 1ZII 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=1ZII OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Alber, T.]] | [[Category: Alber, T.]] | ||
| - | [[Category: Brown, R | + | [[Category: Brown, R A.]] |
| - | [[Category: Junior, L | + | [[Category: Junior, L Gonzalez.]] |
[[Category: Richardson, D.]] | [[Category: Richardson, D.]] | ||
[[Category: ACE]] | [[Category: ACE]] | ||
| Line 26: | Line 26: | ||
[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''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
|
GCN4-LEUCINE ZIPPER CORE MUTANT ASN16ABA IN THE DIMERIC 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
1ZII 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
Page seeded by OCA on Thu Feb 21 16:15:52 2008
