1gcm
From Proteopedia
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| - | [[Image:1gcm.gif|left|200px]] | + | [[Image:1gcm.gif|left|200px]] |
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| - | '''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= | ||
| + | }} | ||
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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== | ||
| - | 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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| 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
Page seeded by OCA on Thu Mar 20 11:21:23 2008
