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Crystal structures of a single coiled-coil peptide in two oligomeric states reveal the basis for structural polymorphism.

Gonzalez L, Brown RA, Richardson D, Alber T
Nat Struct Biol 3 1002-9 (1996)
Related entries: 1gcl, 1swi, 1zij, 2zta

Cited: 60 times
EuropePMC logo PMID: 8946853

Abstract

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.

Articles - 1zii mentioned but not cited (2)

  1. Electrostatic contributions to the stability of the GCN4 leucine zipper structure. Matousek WM, Ciani B, Fitch CA, Garcia-Moreno B, Kammerer RA, Alexandrescu AT. J. Mol. Biol. 374 206-219 (2007)
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Reviews citing this publication (6)

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Articles citing this publication (52)

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Related citations provided by authors (4)

  1. An engineered allosteric switch in leucine-zipper oligomerization.. Gonzalez L, Plecs JJ, Alber T Nat Struct Biol 3 510-5 (1996)
  2. Crystal Structure of an Isoleucine-Zipper Trimer. Harbury PB, Kim PS, Alber T Nature 371 80- (1994)
  3. A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants.. Harbury PB, Zhang T, Kim PS, Alber T Science 262 1401-7 (1993)
  4. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil.. O'Shea EK, Klemm JD, Kim PS, Alber T Science 254 539-44 (1991)

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