Analysis of alpha-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation.

  title={Analysis of alpha-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation.},
  author={Sergei V. Strelkov and Peter Burkhard},
  journal={Journal of structural biology},
  volume={137 1-2},
Alpha-helical coiled coils represent a widespread protein structure motif distinguished by a seven-residue periodicity of apolar residues in the primary sequence. A characteristic "knobs-into-holes" packing of these residues into a hydrophobic core results in a superhelical, usually left-handed, rope of two or more alpha-helices. Such a geometry can be parameterized. For this purpose, a new computer program, TWISTER, was developed. With the three-dimensional coordinates as input, TWISTER uses… 

A seven-helix coiled coil

It is demonstrated that heptad repeats containing four hydrophobic positions can direct assembly of complex, higher-order coiled-coil structures with rich diversity for close packing of α-helices.

A library of coiled-coil domains: from regular bundles to peculiar twists

SamCC-Turbo, a software for fully automated, per-residue measurement of coiled coils, is developed and a comprehensive atlas of ∼50 000 coiled-coil regions is generated, which features precise measurements as well as decomposes coil structures into fragments characterized by various degrees of supercoiling.

α/β coiled coils

The results show that a substantially novel backbone structure is possible within the allowed regions of the Ramachandran space with only minor mutations to a known fold.

The Structure and Topology of α-Helical Coiled Coils

The principles by which coiled coils are structured are outlined, the determinants of their folding and stability are reviewed, and an overview of their diverse architectures are presented.

How sequence directs bending in tropomyosin and other two‐stranded alpha‐helical coiled coils

  • Jerry H. Brown
  • Chemistry
    Protein science : a publication of the Protein Society
  • 2010
Comparison of tropomyosin structures determined in independent crystal environments provides further evidence for the concept that sequence directs the bending of the coiled coil, but that crystal environment is at least as important as sequence for determining the magnitude of bending.

Socket: a program for identifying and analysing coiled-coil motifs within protein structures.

SOCKET, a computer program to identify heptad repeats of different motifs automatically in protein structures, was developed and a set of unambiguous coiled-coil structures retrieved from the RCSB Protein Data Bank was gathered.

Buried polar residues in coiled-coil interfaces.

Variants of the well-characterized coiled coil GCN4-p1 are constructed with a single polar residue at either an a or a d position, showing how single polar residues in the interface affect not only local packing, but also overall coiled-coil geometry as seen in the Crick supercoil parameters and core cavity volumes.

Pitch diversity in α‐helical coiled coils

Two complementary methods for measuring local pitch based on heptad position in α‐helical coiled coils are described and applied to six crystal structures. The results reveal a diversity of pitch

Heptad breaks in α‐helical coiled coils: Stutters and stammers

It is shown how, in other cases, stammers would lead to overwinding of the supercoil, and it is suggested that such non‐close‐packed cores may function to terminate certain coiled‐coil regions, and may also account for the flexibility observed in such long α‐fibrous molecules as myosin.

Crystal structure of an isoleucine-zipper trimer

SUBUNIT oligomerization in many proteins is mediated by short coiled-coil motifs1,2. These motifs share a characteristic seven-amino-acid repeat containing hydrophobic residues at the first (a) and

Predicting coiled-coil regions in proteins.

  • A. Lupas
  • Chemistry, Physics
    Current opinion in structural biology
  • 1997

X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil.

The crystal structure of the GCN4Leucine zipper suggests a key role for the leucine repeat, but also shows how other features of the coiled coil contribute to dimer formation.