1gcm
From Proteopedia
(New page: 200px<br /><applet load="1gcm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gcm, resolution 1.8Å" /> '''GCN4 LEUCINE ZIPPER C...) |
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| - | [[Image:1gcm.gif|left|200px]]<br /><applet load="1gcm" size=" | + | [[Image:1gcm.gif|left|200px]]<br /><applet load="1gcm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gcm, resolution 1.8Å" /> | caption="1gcm, resolution 1.8Å" /> | ||
'''GCN4 LEUCINE ZIPPER CORE MUTANT P-LI'''<br /> | '''GCN4 LEUCINE ZIPPER CORE MUTANT P-LI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Subunit oligomerization in many proteins is mediated by short coiled-coil | + | 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== | ==About this Structure== | ||
| - | 1GCM 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]. Full crystallographic information is available from [http:// | + | 1GCM 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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Alber, T.]] | [[Category: Alber, T.]] | ||
| - | [[Category: Harbury, P | + | [[Category: Harbury, P B.]] |
| - | [[Category: Kim, P | + | [[Category: Kim, P S.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: hydrophobic core mutant]] | [[Category: hydrophobic core mutant]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:43 2008'' |
Revision as of 10:48, 21 February 2008
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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 with as ligand. 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 Feb 21 12:48:43 2008
