1GK6

Human vimentin coil 2B fragment linked to GCN4 leucine zipper (Z2B)

Replaces:  1E7T

Summary for 1GK6

• Entry DOI: 10.2210/pdb1gk6/pdb
• Related: 1GK4 1GK7 2ZTA
• Descriptor: VIMENTIN (2 entities in total)
• Functional Keywords: structural protein, intermediate filament, dimer, parallel coiled coil, heptad repeat, leucine zipper, fusion protein
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Total number of polymer chains: 2
• Total formula weight: 13852.13

Authors

Strelkov, S.V.,Herrmann, H.,Geisler, N.,Zimbelmann, R.,Aebi, U.,Burkhard, P. (deposition date: 2001-08-08, release date: 2002-03-15, Last modification date: 2023-12-13)

Primary citation

Strelkov, S.,Herrmann, H.,Geisler, N.,Wedig, T.,Zimbelmann, R.,Aebi, U.,Burkhard, P.
Conserved Segments 1A and 2B of the Intermediate Filament Dimer: Their Atomic Structures and Role in Filament Assembly.
Embo J., 21:1255-, 2002

PubMed Abstract: Intermediate filaments (IFs) are key components of the cytoskeleton in higher eukaryotic cells. The elementary IF 'building block' is an elongated coiled-coil dimer consisting of four consecutive alpha-helical segments. The segments 1A and 2B include highly conserved sequences and are critically involved in IF assembly. Based on the crystal structures of three human vimentin fragments at 1.4-2.3 A resolution (PDB entries 1gk4, 1gk6 and 1gk7), we have established the molecular organization of these two segments. The fragment corresponding to segment 1A forms a single, amphipatic alpha-helix, which is compatible with a coiled-coil geometry. While this segment might yield a coiled coil within an isolated dimer, monomeric 1A helices are likely to play a role in specific dimer-dimer interactions during IF assembly. The 2B segment reveals a double-stranded coiled coil, which unwinds near residue Phe351 to accommodate a 'stutter'. A fragment containing the last seven heptads of 2B interferes heavily with IF assembly and also transforms mature vimentin filaments into a new kind of structure. These results provide the first insight into the architecture and functioning of IFs at the atomic level.

PubMed: 11889032
DOI: 10.1093/EMBOJ/21.6.1255

Experimental method

X-RAY DIFFRACTION (1.9 Å)