2gus
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2gus.gif|left|200px]] | [[Image:2gus.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2gus", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_2gus| PDB=2gus | 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''' | ||
| Line 30: | Line 27: | ||
[[Category: Lu, M.]] | [[Category: Lu, M.]] | ||
[[Category: Zheng, Q.]] | [[Category: Zheng, Q.]] | ||
| - | [[Category: | + | [[Category: Coiled coil]] |
| - | [[Category: | + | [[Category: Lipoprotein]] |
| - | [[Category: | + | [[Category: Phenylalanine-zipper]] |
| - | [[Category: | + | [[Category: Protein folding]] |
| - | [[Category: | + | [[Category: Tetramer]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:33:46 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 02:33, 4 May 2008
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.
About this Structure
2GUS 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 Sun May 4 05:33:46 2008
