1gcm: Difference between revisions
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[[Image:1gcm.gif|left|200px]] | [[Image:1gcm.gif|left|200px]] | ||
'''GCN4 LEUCINE ZIPPER CORE MUTANT P-LI''' | {{Structure | ||
|PDB= 1gcm |SIZE=350|CAPTION= <scene name='initialview01'>1gcm</scene>, resolution 1.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''GCN4 LEUCINE ZIPPER CORE MUTANT P-LI''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1GCM is a [ | 1GCM 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=1GCM OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of an isoleucine-zipper trimer., Harbury PB, Kim PS, Alber T, Nature. 1994 Sep 1;371(6492):80-3. PMID:[http:// | Crystal structure of an isoleucine-zipper trimer., Harbury PB, Kim PS, Alber T, Nature. 1994 Sep 1;371(6492):80-3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8072533 8072533] | ||
[[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 11:21:23 2008'' | ||
Revision as of 09:21, 20 March 2008
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| 1gcm, resolution 1.8Å | |||||||||||||
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| Ligands: | ACE | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
GCN4 LEUCINE ZIPPER CORE MUTANT P-LI
Overview
Subunit oligomerization in many proteins is mediated by short coiled-coil motifs. These motifs share a characteristic seven-amino-acid repeat containing hydrophobic residues at the first (a) and fourth (d) positions. Despite this common pattern, different sequences form two-, three- and four-stranded helical ropes. We have investigated the basis for oligomer choice by characterizing variants of the GCN4 leucine-zipper dimerization domain that adopt trimeric or tetrameric structures in response to mutations at the a and d positions. We now report the high-resolution X-ray crystal structure of an isoleucine-containing mutant that folds into a parallel three-stranded, alpha-helical coiled coil. In contrast to the dimer and tetramer structures, the interior packing of the trimer can accommodate beta-branched residues in the most preferred rotamer at both hydrophobic positions. Compatibility of the shape of the core amino acids with the distinct packing spaces in the two-, three- and four-stranded conformations appears to determine the oligomerization state of the GCN4 leucine-zipper variants.
About this Structure
1GCM is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of an isoleucine-zipper trimer., Harbury PB, Kim PS, Alber T, Nature. 1994 Sep 1;371(6492):80-3. PMID:8072533
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