1ce9
From Proteopedia
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ce9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ce9 OCA], [http://www.ebi.ac.uk/pdbsum/1ce9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ce9 RCSB]</span> | ||
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[[Category: thermal stability]] | [[Category: thermal stability]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:19:57 2008'' |
Revision as of 16:20, 30 March 2008
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| , resolution 1.8Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HELIX CAPPING IN THE GCN4 LEUCINE ZIPPER
Overview
Capping interactions associated with specific sequences at or near the ends of alpha-helices are important determinants of the stability of protein secondary and tertiary structure. We investigate here the role of the helix-capping motif Ser-X-X-Glu, a sequence that occurs frequently at the N termini of alpha helices in proteins, on the conformation and stability of the GCN4 leucine zipper. The 1.8 A resolution crystal structure of the capped molecule reveals distinct conformations, packing geometries and hydrogen-bonding networks at the amino terminus of the two helices in the leucine zipper dimer. The free energy of helix stabilization associated with the hydrogen-bonding and hydrophobic interactions in this capping structure is -1.2 kcal/mol, evaluated from thermal unfolding experiments. A single cap thus contributes appreciably to stabilizing the terminated helix and thereby the native state. These results suggest that helix capping plays a further role in protein folding, providing a sensitive connector linking alpha-helix formation to the developing tertiary structure of a protein.
About this Structure
1CE9 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Helix capping in the GCN4 leucine zipper., Lu M, Shu W, Ji H, Spek E, Wang L, Kallenbach NR, J Mol Biol. 1999 May 14;288(4):743-52. PMID:10329176
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