2zta
From Proteopedia
(New page: 200px<br /> <applet load="2zta" size="450" color="white" frame="true" align="right" spinBox="true" caption="2zta, resolution 1.8Å" /> '''X-RAY STRUCTURE OF T...) |
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| - | [[Image:2zta.gif|left|200px]]<br /> | + | [[Image:2zta.gif|left|200px]]<br /><applet load="2zta" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2zta" size=" | + | |
caption="2zta, resolution 1.8Å" /> | caption="2zta, resolution 1.8Å" /> | ||
'''X-RAY STRUCTURE OF THE GCN4 LEUCINE ZIPPER, A TWO-STRANDED, PARALLEL COILED COIL'''<br /> | '''X-RAY STRUCTURE OF THE GCN4 LEUCINE ZIPPER, A TWO-STRANDED, PARALLEL COILED COIL'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The x-ray crystal structure of a peptide corresponding to the leucine | + | The x-ray crystal structure of a peptide corresponding to the leucine zipper of the yeast transcriptional activator GCN4 has been determined at 1.8 angstrom resolution. The peptide forms a parallel, two-stranded coiled coil of alpha helices packed as in the "knobs-into-holes" model proposed by Crick in 1953. Contacts between the helices include ion pairs and an extensive hydrophobic interface that contains a distinctive hydrogen bond. The conserved leucines, like the residues in the alternate hydrophobic repeat, make side-to-side interactions (as in a handshake) in every other layer of the dimer interface. The crystal structure of the GCN4 leucine zipper suggests a key role for the leucine repeat, but also shows how other features of the coiled coil contribute to dimer formation. |
==About this Structure== | ==About this Structure== | ||
| - | 2ZTA 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]. The following page contains interesting information on the relation of 2ZTA with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb70_1.html Designer Proteins]]. Full crystallographic information is available from [http:// | + | 2ZTA 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]. The following page contains interesting information on the relation of 2ZTA with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb70_1.html Designer Proteins]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZTA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Alber, T.]] | [[Category: Alber, T.]] | ||
| - | [[Category: Kim, P | + | [[Category: Kim, P S.]] |
| - | [[Category: Klemm, J | + | [[Category: Klemm, J D.]] |
| - | [[Category: Shea, E | + | [[Category: Shea, E K.O.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: leucine zipper]] | [[Category: leucine zipper]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:01:46 2008'' |
Revision as of 17:01, 21 February 2008
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X-RAY STRUCTURE OF THE GCN4 LEUCINE ZIPPER, A TWO-STRANDED, PARALLEL COILED COIL
Overview
The x-ray crystal structure of a peptide corresponding to the leucine zipper of the yeast transcriptional activator GCN4 has been determined at 1.8 angstrom resolution. The peptide forms a parallel, two-stranded coiled coil of alpha helices packed as in the "knobs-into-holes" model proposed by Crick in 1953. Contacts between the helices include ion pairs and an extensive hydrophobic interface that contains a distinctive hydrogen bond. The conserved leucines, like the residues in the alternate hydrophobic repeat, make side-to-side interactions (as in a handshake) in every other layer of the dimer interface. The crystal structure of the GCN4 leucine zipper suggests a key role for the leucine repeat, but also shows how other features of the coiled coil contribute to dimer formation.
About this Structure
2ZTA is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. The following page contains interesting information on the relation of 2ZTA with [Designer Proteins]. Full crystallographic information is available from OCA.
Reference
X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil., O'Shea EK, Klemm JD, Kim PS, Alber T, Science. 1991 Oct 25;254(5031):539-44. PMID:1948029
Page seeded by OCA on Thu Feb 21 19:01:46 2008
