1C94

REVERSING THE SEQUENCE OF THE GCN4 LEUCINE ZIPPER DOES NOT AFFECT ITS FOLD.

Summary for 1C94

• Entry DOI: 10.2210/pdb1c94/pdb
• Descriptor: RETRO-GCN4 LEUCINE ZIPPER (2 entities in total)
• Functional Keywords: retro-coiled coil, 4-alpha-helix-bundle, peptide synthesis, gene regulation
• Total number of polymer chains: 2
• Total formula weight: 8928.39

Authors

Mittl, P.R.E.,Deillon, C.A.,Sargent, D.,Liu, N.,Klauser, S.,Thomas, R.M.,Gutte, B.,Gruetter, M.G. (deposition date: 1999-07-30, release date: 2000-03-22, Last modification date: 2024-02-07)

Primary citation

Mittl, P.R.,Deillon, C.,Sargent, D.,Liu, N.,Klauser, S.,Thomas, R.M.,Gutte, B.,Grutter, M.G.
The retro-GCN4 leucine zipper sequence forms a stable three-dimensional structure.
Proc.Natl.Acad.Sci.USA, 97:2562-2566, 2000

PubMed Abstract: The question of whether a protein whose natural sequence is inverted adopts a stable fold is still under debate. We have determined the 2. 1-A crystal structure of the retro-GCN4 leucine zipper. In contrast to the two-stranded helical coiled-coil GCN4 leucine zipper, the retro-leucine zipper formed a very stable, parallel four-helix bundle, which now lends itself to further structural and functional studies.

PubMed: 10716989
DOI: 10.1073/pnas.97.6.2562

Experimental method

X-RAY DIFFRACTION (2.08 Å)