2nrn
From Proteopedia
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|PDB= 2nrn |SIZE=350|CAPTION= <scene name='initialview01'>2nrn</scene>, resolution 1.40Å | |PDB= 2nrn |SIZE=350|CAPTION= <scene name='initialview01'>2nrn</scene>, resolution 1.40Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2b1f|2B1F]], [[2hy6|2HY6]], [[2b22|2B22]], [[2ipz|2IPZ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nrn OCA], [http://www.ebi.ac.uk/pdbsum/2nrn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nrn RCSB]</span> | ||
}} | }} | ||
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[[Category: Liu, J.]] | [[Category: Liu, J.]] | ||
[[Category: Lu, M.]] | [[Category: Lu, M.]] | ||
| - | [[Category: PO4]] | ||
[[Category: coiled coil]] | [[Category: coiled coil]] | ||
[[Category: protein design]] | [[Category: protein design]] | ||
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[[Category: tetramer]] | [[Category: tetramer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:07:17 2008'' |
Revision as of 01:07, 31 March 2008
| |||||||
| , resolution 1.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | GCN4, AAS3, ARG9 (Saccharomyces cerevisiae) | ||||||
| Related: | 2B1F, 2HY6, 2B22, 2IPZ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant
Overview
The hydrophobic core of the GCN4 leucine-zipper dimerization domain is formed by a parallel helical association between nonpolar side chains at the a and d positions of the heptad repeat. Here we report a self-assembling coiled-coil array formed by the GCN4-pAe peptide that differs from the wild-type GCN4 leucine zipper by alanine substitutions at three charged e positions. GCN4-pAe is incompletely folded in normal solution conditions yet self-assembles into an antiparallel tetraplex in crystals by formation of unanticipated hydrophobic seams linking the last two heptads of two parallel double-stranded coiled coils. The GCN4-pAe tetramers in the lattice associate laterally through the identical interactions to those in the intramolecular dimer-dimer interface. The van der Waals packing interaction in the solid state controls extended supramolecular assembly of the protein, providing an unusual atomic scale view of a mesostructure.
About this Structure
2NRN is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant., Deng Y, Zheng Q, Liu J, Cheng CS, Kallenbach NR, Lu M, Protein Sci. 2007 Feb;16(2):323-8. Epub 2006 Dec 22. PMID:17189475
Page seeded by OCA on Mon Mar 31 04:07:17 2008
