2b22

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|PDB= 2b22 |SIZE=350|CAPTION= <scene name='initialview01'>2b22</scene>, resolution 2.00&Aring;
|PDB= 2b22 |SIZE=350|CAPTION= <scene name='initialview01'>2b22</scene>, resolution 2.00&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
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|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= GCN4, AAS3, ARG9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
|GENE= GCN4, AAS3, ARG9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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|DOMAIN=
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|RELATEDENTRY=[[2zta|2ZTA]], [[1gcm|1GCM]], [[1gcl|1GCL]], [[2b1f|2B1F]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b22 OCA], [http://www.ebi.ac.uk/pdbsum/2b22 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b22 RCSB]</span>
}}
}}
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[[Category: Lu, M.]]
[[Category: Lu, M.]]
[[Category: Zheng, Q.]]
[[Category: Zheng, Q.]]
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[[Category: NA]]
 
[[Category: ala coil]]
[[Category: ala coil]]
[[Category: antiparallel tetramer]]
[[Category: antiparallel tetramer]]
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[[Category: protein structure]]
[[Category: protein structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:56:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:00:24 2008''

Revision as of 23:00, 30 March 2008


PDB ID 2b22

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands:
Gene: GCN4, AAS3, ARG9 (Saccharomyces cerevisiae)
Related: 2ZTA, 1GCM, 1GCL, 2B1F


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat


Overview

Coiled-coil sequences in proteins commonly share a seven-amino acid repeat with nonpolar side chains at the first (a) and fourth (d) positions. We investigate here the role of a 3-3-1 hydrophobic repeat containing nonpolar amino acids at the a, d, and g positions in determining the structures of coiled coils using mutants of the GCN4 leucine zipper dimerization domain. When three charged residues at the g positions in the parental sequence are replaced by nonpolar alanine or valine side chains, stable four-helix structures result. The X-ray crystal structures of the tetramers reveal antiparallel, four-stranded coiled coils in which the a, d, and g side chains interlock in a combination of knobs-into-knobs and knobs-into-holes packing. Interfacial interactions in a coiled coil can therefore be prescribed by hydrophobic-polar patterns beyond the canonical 3-4 heptad repeat. The results suggest that the conserved, charged residues at the g positions in the GCN4 leucine zipper can impart a negative design element to disfavor thermodynamically more stable, antiparallel tetramers.

About this Structure

2B22 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat., Deng Y, Liu J, Zheng Q, Eliezer D, Kallenbach NR, Lu M, Structure. 2006 Feb;14(2):247-55. PMID:16472744

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