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2guv

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{{STRUCTURE_2guv| PDB=2guv | SCENE= }}
{{STRUCTURE_2guv| PDB=2guv | SCENE= }}
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'''Conformational Transition between Four- and Five-stranded Phenylalanine Zippers Determined by a Local Packing Interaction'''
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===Conformational Transition between Four- and Five-stranded Phenylalanine Zippers Determined by a Local Packing Interaction===
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==Overview==
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Alpha-helical coiled coils play a crucial role in mediating specific protein-protein interactions. However, the rules and mechanisms that govern helix-helix association in coiled coils remain incompletely understood. Here we have engineered a seven heptad "Phe-zipper" protein (Phe-14) with phenylalanine residues at all 14 hydrophobic a and d positions, and generated a further variant (Phe-14(M)) in which a single core Phe residue is substituted with Met. Phe-14 forms a discrete alpha-helical pentamer in aqueous solution, while Phe-14(M) folds into a tetrameric helical structure. X-ray crystal structures reveal that in both the tetramer and the pentamer the a and d side-chains interlock in a classical knobs-into-holes packing to produce parallel coiled-coil structures enclosing large tubular cavities. However, the presence of the Met residue in the apolar interface of the tetramer markedly alters its local coiled-coil conformation and superhelical geometry. Thus, short-range interactions involving the Met side-chain serve to preferentially select for tetramer formation, either by inhibiting a nucleation step essential for pentamer folding or by abrogating an intermediate required to form the pentamer. Although specific trigger sequences have not been clearly identified in dimeric coiled coils, higher-order coiled coils, as well as other oligomeric multi-protein complexes, may require such sequences to nucleate and direct their assembly.
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(as it appears on PubMed at http://www.pubmed.gov), where 16828114 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16828114}}
==About this Structure==
==About this Structure==
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[[Category: Phenylalanine-zipper]]
[[Category: Phenylalanine-zipper]]
[[Category: Protein folding]]
[[Category: Protein folding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:33:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:06:22 2008''

Revision as of 06:06, 29 July 2008

Image:2guv.png

Template:STRUCTURE 2guv

Conformational Transition between Four- and Five-stranded Phenylalanine Zippers Determined by a Local Packing Interaction

Template:ABSTRACT PUBMED 16828114

About this Structure

2GUV is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Conformational transition between four and five-stranded phenylalanine zippers determined by a local packing interaction., Liu J, Zheng Q, Deng Y, Kallenbach NR, Lu M, J Mol Biol. 2006 Aug 4;361(1):168-79. Epub 2006 Jun 13. PMID:16828114

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