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2hy6

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[[Image:2hy6.jpg|left|200px]]
[[Image:2hy6.jpg|left|200px]]
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{{Structure
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|PDB= 2hy6 |SIZE=350|CAPTION= <scene name='initialview01'>2hy6</scene>, resolution 1.25&Aring;
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|SITE=
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|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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{{STRUCTURE_2hy6| PDB=2hy6 | SCENE= }}
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|RELATEDENTRY=[[2zta|2ZTA]], [[1gcm|1GCM]], [[1gcl|1GCL]], [[2b1f|2B1F]], [[2b22|2B22]]
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|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>
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'''A seven-helix coiled coil'''
'''A seven-helix coiled coil'''
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[[Category: Lu, M.]]
[[Category: Lu, M.]]
[[Category: Zheng, Q.]]
[[Category: Zheng, Q.]]
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[[Category: coiled coil]]
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[[Category: Coiled coil]]
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[[Category: parallel heptamer]]
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[[Category: Parallel heptamer]]
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[[Category: protein design]]
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[[Category: Protein design]]
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[[Category: protein structure]]
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[[Category: Protein structure]]
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Revision as of 03:51, 4 May 2008

Template:STRUCTURE 2hy6

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 Sun May 4 06:51:29 2008

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