2hy6
From Proteopedia
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| - | [[Image:2hy6.jpg|left|200px]] | + | [[Image:2hy6.jpg|left|200px]] |
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| - | '''A seven-helix coiled coil''' | + | {{Structure |
| + | |PDB= 2hy6 |SIZE=350|CAPTION= <scene name='initialview01'>2hy6</scene>, resolution 1.25Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= GCN4, AAS3, ARG9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | }} | ||
| + | |||
| + | '''A seven-helix coiled coil''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2HY6 is a [ | + | 2HY6 is a [[Single protein]] structure of 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=2HY6 OCA]. |
==Reference== | ==Reference== | ||
| - | A seven-helix coiled coil., Liu J, Zheng Q, Deng Y, Cheng CS, Kallenbach NR, Lu M, Proc Natl Acad Sci U S A. 2006 Oct 17;103(42):15457-62. Epub 2006 Oct 9. PMID:[http:// | + | A seven-helix coiled coil., Liu J, Zheng Q, Deng Y, Cheng CS, Kallenbach NR, Lu M, Proc Natl Acad Sci U S A. 2006 Oct 17;103(42):15457-62. Epub 2006 Oct 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17030805 17030805] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protein structure]] | [[Category: protein structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:23:06 2008'' |
Revision as of 15:23, 20 March 2008
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| , resolution 1.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | GCN4, AAS3, ARG9 (Saccharomyces cerevisiae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
A seven-helix coiled coil
Overview
Coiled-coil proteins contain a characteristic seven-residue sequence repeat whose positions are designated a to g. The interacting surface between alpha-helices in a classical coiled coil is formed by interspersing nonpolar side chains at the a and d positions with hydrophilic residues at the flanking e and g positions. To explore how the chemical nature of these core amino acids dictates the overall coiled-coil architecture, we replaced all eight e and g residues in the GCN4 leucine zipper with nonpolar alanine side chains. Surprisingly, the alanine-containing mutant forms a stable alpha-helical heptamer in aqueous solution. The 1.25-A resolution crystal structure of the heptamer reveals a parallel seven-stranded coiled coil enclosing a large tubular channel with an unusual heptad register shift between adjacent staggered helices. The overall geometry comprises two interleaved hydrophobic helical screws of interacting cross-sectional a and d layers that have not been seen before. Moreover, asparagines at the a positions play an essential role in heptamer formation by participating in a set of buried interhelix hydrogen bonds. These results demonstrate that heptad repeats containing four hydrophobic positions can direct assembly of complex, higher-order coiled-coil structures with rich diversity for close packing of alpha-helices.
About this Structure
2HY6 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
A seven-helix coiled coil., Liu J, Zheng Q, Deng Y, Cheng CS, Kallenbach NR, Lu M, Proc Natl Acad Sci U S A. 2006 Oct 17;103(42):15457-62. Epub 2006 Oct 9. PMID:17030805
Page seeded by OCA on Thu Mar 20 17:23:06 2008
