2hy6
From Proteopedia
| Line 7: | Line 7: | ||
|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=[[2zta|2ZTA]], [[1gcm|1GCM]], [[1gcl|1GCL]], [[2b1f|2B1F]], [[2b22|2B22]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hy6 OCA], [http://www.ebi.ac.uk/pdbsum/2hy6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hy6 RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Lu, M.]] | [[Category: Lu, M.]] | ||
[[Category: Zheng, Q.]] | [[Category: Zheng, Q.]] | ||
| - | [[Category: HEZ]] | ||
[[Category: coiled coil]] | [[Category: coiled coil]] | ||
[[Category: parallel heptamer]] | [[Category: parallel heptamer]] | ||
| Line 34: | Line 36: | ||
[[Category: protein structure]] | [[Category: protein structure]] | ||
| - | ''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 03:37:07 2008'' |
Revision as of 00:37, 31 March 2008
| |||||||
| , resolution 1.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | GCN4, AAS3, ARG9 (Saccharomyces cerevisiae) | ||||||
| Related: | 2ZTA, 1GCM, 1GCL, 2B1F, 2B22
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Mon Mar 31 03:37:07 2008
