2IPZ

A Parallel Coiled-Coil Tetramer with Offset Helices

Summary for 2IPZ

• Entry DOI: 10.2210/pdb2ipz/pdb
• Related: 2B1F 2B22 2HY6 2ZTA
• Descriptor: General control protein GCN4, GLYCEROL, ISOPROPYL ALCOHOL, ... (4 entities in total)
• Functional Keywords: coiled coils, protein design, parallel tetramer, protein structure, biosynthetic protein
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus: P03069
• Total number of polymer chains: 4
• Total formula weight: 16099.25

Authors

Liu, J.,Lu, M. (deposition date: 2006-10-12, release date: 2007-01-16, Last modification date: 2023-08-30)

Primary citation

Liu, J.,Deng, Y.,Zheng, Q.,Cheng, C.S.,Kallenbach, N.R.,Lu, M.
A Parallel Coiled-Coil Tetramer with Offset Helices.
Biochemistry, 45:15224-15231, 2006

PubMed Abstract: Specific helix-helix interactions are fundamental in assembling the native state of proteins and in protein-protein interfaces. Coiled coils afford a unique model system for elucidating principles of molecular recognition between alpha helices. The coiled-coil fold is specified by a characteristic seven amino acid repeat containing hydrophobic residues at the first (a) and fourth (d) positions. Nonpolar side chains spaced three and four residues apart are referred to as the 3-4 hydrophobic repeat. The presence of apolar amino acids at the e or g positions (corresponding to a 3-3-1 hydrophobic repeat) can provide new possibilities for close-packing of alpha-helices that includes examples such as the lac repressor tetramerization domain. Here we demonstrate that an unprecedented coiled-coil interface results from replacement of three charged residues at the e positions in the dimeric GCN4 leucine zipper by nonpolar valine side chains. Equilibrium circular dichroism and analytical ultracentrifugation studies indicate that the valine-containing mutant forms a discrete alpha-helical tetramer with a significantly higher stability than the parent leucine-zipper molecule. The 1.35 A resolution crystal structure of the tetramer reveals a parallel four-stranded coiled coil with a three-residue interhelical offset. The local packing geometry of the three hydrophobic positions in the tetramer conformation is completely different from that seen in classical tetrameric structures yet bears resemblance to that in three-stranded coiled coils. These studies demonstrate that distinct van der Waals interactions beyond the a and d side chains can generate a diverse set of helix-helix interfaces and three-dimensional supercoil structures.

PubMed: 17176044
DOI: 10.1021/bi061914m

Experimental method

X-RAY DIFFRACTION (1.35 Å)