1zij
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(New page: 200px<br /><applet load="1zij" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zij, resolution 2.00Å" /> '''GCN4-LEUCINE ZIPPER ...)
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Revision as of 05:21, 21 November 2007
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GCN4-LEUCINE ZIPPER CORE MUTANT ASN16ABA IN THE TRIMERIC 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
1ZIJ is a Single protein structure of sequence from Saccharomyces cerevisiae with ACE 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
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