1gcl
From Proteopedia
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| - | [[Image:1gcl.jpg|left|200px]] | + | [[Image:1gcl.jpg|left|200px]] |
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| - | '''GCN4 LEUCINE ZIPPER CORE MUTANT P-LI''' | + | {{Structure |
| + | |PDB= 1gcl |SIZE=350|CAPTION= <scene name='initialview01'>1gcl</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''GCN4 LEUCINE ZIPPER CORE MUTANT P-LI''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GCL is a [ | + | 1GCL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCL OCA]. |
==Reference== | ==Reference== | ||
| - | A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants., Harbury PB, Zhang T, Kim PS, Alber T, Science. 1993 Nov 26;262(5138):1401-7. PMID:[http:// | + | A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants., Harbury PB, Zhang T, Kim PS, Alber T, Science. 1993 Nov 26;262(5138):1401-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8248779 8248779] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrophobic core mutant]] | [[Category: hydrophobic core mutant]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:21:20 2008'' |
Revision as of 09:21, 20 March 2008
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| , resolution 2.1Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
GCN4 LEUCINE ZIPPER CORE MUTANT P-LI
Overview
Coiled-coil sequences in proteins consist of heptad repeats containing two characteristic hydrophobic positions. The role of these buried hydrophobic residues in determining the structures of coiled coils was investigated by studying mutants of the GCN4 leucine zipper. When sets of buried residues were altered, two-, three-, and four-helix structures were formed. The x-ray crystal structure of the tetramer revealed a parallel, four-stranded coiled coil. In the tetramer conformation, the local packing geometry of the two hydrophobic positions in the heptad repeat is reversed relative to that in the dimer. These studies demonstrate that conserved, buried residues in the GCN4 leucine zipper direct dimer formation. In contrast to proposals that the pattern of hydrophobic and polar amino acids in a protein sequence is sufficient to determine three-dimensional structure, the shapes of buried side chains in coiled coils are essential determinants of the global fold.
About this Structure
1GCL is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants., Harbury PB, Zhang T, Kim PS, Alber T, Science. 1993 Nov 26;262(5138):1401-7. PMID:8248779
Page seeded by OCA on Thu Mar 20 11:21:20 2008
