1kfn
From Proteopedia
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'''Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants''' | '''Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants''' | ||
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[[Category: Liu, J.]] | [[Category: Liu, J.]] | ||
[[Category: Lu, M.]] | [[Category: Lu, M.]] | ||
| - | [[Category: | + | [[Category: Alanine-zipper]] |
| - | [[Category: | + | [[Category: Coiled coil]] |
| - | [[Category: | + | [[Category: Helix capping]] |
| - | [[Category: | + | [[Category: Lipoprotein]] |
| - | [[Category: | + | [[Category: Protein folding]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:41:22 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:41, 2 May 2008
Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants
Overview
Native proteins exhibit precise geometric packing of atoms in their hydrophobic interiors. Nonetheless, controversy remains about the role of core side-chain packing in specifying and stabilizing the folded structures of proteins. Here we investigate the role of core packing in determining the conformation and stability of the Lpp-56 trimerization domain. The X-ray crystal structures of Lpp-56 mutants with alanine substitutions at two and four interior core positions reveal trimeric coiled coils in which the twist of individual helices and the helix-helix spacing vary significantly to achieve the most favored superhelical packing arrangement. Introduction of each alanine "layer" into the hydrophobic core destabilizes the superhelix by 1.4 kcal mol(-1). Although the methyl groups of the alanine residues pack at their optimum van der Waals contacts in the coiled-coil trimer, they provide a smaller component of hydrophobic interactions than bulky hydrophobic side-chains to the thermodynamic stability. Thus, specific side-chain packing in the hydrophobic core of coiled coils are important determinants of protein main-chain conformation and stability.
About this Structure
1KFN is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants., Liu J, Cao W, Lu M, J Mol Biol. 2002 May 3;318(3):877-88. PMID:12054830 Page seeded by OCA on Fri May 2 22:41:22 2008
