3KLT

Crystal structure of a vimentin fragment

Summary for 3KLT

• Entry DOI: 10.2210/pdb3klt/pdb
• Descriptor: Vimentin, 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL, SAMARIUM (III) ION, ... (9 entities in total)
• Functional Keywords: 2a, l2, alpha-helix, coiled-coil, parallel helices, coiled coil, intermediate filament, vimentin, structural protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 4
• Total formula weight: 35281.50

Authors

Nicolet, S.,Strelkov, S.V. (deposition date: 2009-11-09, release date: 2010-05-26, Last modification date: 2024-03-20)

Primary citation

Nicolet, S.,Herrmann, H.,Aebi, U.,Strelkov, S.V.
Atomic structure of vimentin coil 2.
J.Struct.Biol., 170:369-376, 2010

PubMed Abstract: Intermediate filaments (IFs) are essential cytoskeletal components in metazoan cells. They assemble from elementary dimers that are built around the central alpha-helical coiled-coil rod domain representing the IF 'signature'. The rod consists of two similarly-sized parts, coil 1 and coil 2, connected by a non-alpha-helical linker L12. Coil 2 is absolutely conserved in length across all IF types and was initially predicted to consist of a short coiled-coil segment 2A based on a heptad pattern of hydrophobic residues, another linker L2 and a coiled-coil segment 2B. Here we present the crystal structure of human vimentin fragment including residues 261-335 i.e. approximately the first half of coil 2. The N-terminal part of this fragment reveals a parallel alpha-helical bundle characterized by 3.5 consecutive hendecad repeats. It is immediately followed by a regular left-handed coiled coil. The distinct non-helical linker L2 is therefore not observed. Together with the previously determined crystal structure of the major part of segment 2B (Strelkov et al., 2002), we can now build a complete atomic model of the 21nm long vimentin coil 2 dimer being a relatively rigid rod.

PubMed: 20176112
DOI: 10.1016/j.jsb.2010.02.012

Experimental method

X-RAY DIFFRACTION (2.7 Å)