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1zii

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Revision as of 14:15, 21 February 2008 by OCA (Talk | contribs)
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1zii, resolution 1.8Å

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GCN4-LEUCINE ZIPPER CORE MUTANT ASN16ABA IN THE DIMERIC STATE

Overview

Each protein sequence generally adopts a single native fold, but the sequence features that confer structural uniqueness are not well understood. To define the basis for structural heterogeneity, we determined the high resolution X-ray crystal structures of a single GCN4 leucine-zipper mutant (Asn 16 to aminobutyric acid) in both dimeric and trimeric coiled-coil conformations. The mutant sequence is accommodated in two distinct structures by forming similarly-shaped packing surfaces with different sets of atoms. The trimer structure, in comparison to a previously-characterized trimeric mutant with substitutions in eight core residues, shows that the twist of individual helices and the helix-helix crossing angles can vary significantly to produce the most favoured packing arrangement.

About this Structure

1ZII is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structures of a single coiled-coil peptide in two oligomeric states reveal the basis for structural polymorphism., Gonzalez L Jr, Brown RA, Richardson D, Alber T, Nat Struct Biol. 1996 Dec;3(12):1002-9. PMID:8946853

Page seeded by OCA on Thu Feb 21 16:15:52 2008

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