1gcm
From Proteopedia
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|PDB= 1gcm |SIZE=350|CAPTION= <scene name='initialview01'>1gcm</scene>, resolution 1.8Å | |PDB= 1gcm |SIZE=350|CAPTION= <scene name='initialview01'>1gcm</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gcm OCA], [http://www.ebi.ac.uk/pdbsum/1gcm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gcm RCSB]</span> | ||
}} | }} | ||
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[[Category: Harbury, P B.]] | [[Category: Harbury, P B.]] | ||
[[Category: Kim, P S.]] | [[Category: Kim, P S.]] | ||
| - | [[Category: ACE]] | ||
[[Category: hydrophobic core mutant]] | [[Category: hydrophobic core mutant]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:41:29 2008'' |
Revision as of 17:41, 30 March 2008
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| , resolution 1.8Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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