1gcm: Difference between revisions

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[[~~Image~~:1gcm.~~png|left|200px~~]]

==GCN4 LEUCINE ZIPPER CORE MUTANT P-LI==

== Structural highlights ==

<table><tr><td colspan='2'>[[1gcm]] is a 3 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GCM FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1gcm RCSB], [http://www.ebi.ac.uk/pdbsum/1gcm PDBsum]</span></td></tr>

<table>

== Publication Abstract from PubMed ==

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.

~~{{STRUCTURE_1gcm| PDB=1gcm | SCENE= }}~~

Crystal structure of an isoleucine-zipper trimer.,Harbury PB, Kim PS, Alber T Nature. 1994 Sep 1;371(6492):80-3. PMID:8072533<ref>PMID:8072533</ref>

~~===GCN4 LEUCINE ZIPPER CORE MUTANT P-LI===~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~{{ABSTRACT_PUBMED_8072533}}~~

==See Also==

*[[Gcn4|Gcn4]]

==~~About this Structure~~==

== References ==

[[~~1gcm~~]] ~~is a 3 chain structure with 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].~~

__TOC__

</StructureSection>

[[Category: Saccharomyces cerevisiae]]

[[Category: Alber, T.]]

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@@ Line 1: / Line 1: @@
-[[Image:1gcm.png|left|200px]]
+==GCN4 LEUCINE ZIPPER CORE MUTANT P-LI==
+<StructureSection load='1gcm' size='340' side='right' caption='[[1gcm]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1gcm]] is a 3 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GCM FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1gcm RCSB], [http://www.ebi.ac.uk/pdbsum/1gcm PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-{{STRUCTURE_1gcm|  PDB=1gcm  |  SCENE=  }}
+Crystal structure of an isoleucine-zipper trimer.,Harbury PB, Kim PS, Alber T Nature. 1994 Sep 1;371(6492):80-3. PMID:8072533<ref>PMID:8072533</ref>
-===GCN4 LEUCINE ZIPPER CORE MUTANT P-LI===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_8072533}}
+==See Also==
+*[[Gcn4|Gcn4]]
-==About this Structure==
+== References ==
-[[1gcm]] is a 3 chain structure with 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].
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Saccharomyces cerevisiae]]
 [[Category: Alber, T.]]