From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2guv.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2guv.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2guv| PDB=2guv | SCENE= }} | | {{STRUCTURE_2guv| PDB=2guv | SCENE= }} |
| | | | |
| - | '''Conformational Transition between Four- and Five-stranded Phenylalanine Zippers Determined by a Local Packing Interaction'''
| + | ===Conformational Transition between Four- and Five-stranded Phenylalanine Zippers Determined by a Local Packing Interaction=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16828114}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16828114 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_16828114}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 32: |
Line 36: |
| | [[Category: Phenylalanine-zipper]] | | [[Category: Phenylalanine-zipper]] |
| | [[Category: Protein folding]] | | [[Category: Protein folding]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:33:53 2008'' | + | |
| | + | ''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
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
Page seeded by OCA on Tue Jul 29 09:06:22 2008
