3TRT

Crystal structure of stabilised vimentin coil2 fragment

Summary for 3TRT

• Entry DOI: 10.2210/pdb3trt/pdb
• Related: 3KLT
• Descriptor: Vimentin, SULFATE ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: cytoskeleton, intermediate filament, vimentin, alpha-helix, structural protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 18315.30

Authors

Chernyatina, A.A.,Strelkov, S.V. (deposition date: 2011-09-10, release date: 2012-02-01, Last modification date: 2024-11-27)

Primary citation

Chernyatina, A.A.,Strelkov, S.V.
Stabilization of vimentin coil2 fragment via an engineered disulfide.
J.Struct.Biol., 177:46-53, 2012

PubMed Abstract: Cytoskeletal intermediate filaments (IFs) assemble from the elementary dimers based on a segmented α-helical coiled-coil (CC) structure. Crystallographic studies of IF protein fragments remain the main route to access their atomic structure. To enable crystallization, such fragments must be sufficiently short. As a consequence, they often fail to assemble into the correct CC dimers. In particular, human vimentin fragment D3 corresponding to the first half of coil2 (residues 261-335) stays monomeric in solution. We have induced its dimerization via introducing a disulfide link between two cysteines engineered in the hydrophobic core of the CC close to its N-terminus. The 2.3 Å crystal structure of the D3st (stabilized) fragment reveals a mostly parallel α-helical bundle structure in its N-terminal half which smoothly continues into a left-handed CC towards the C-terminus. This provides a direct evidence for a continuously α-helical structure of the coil2 segment and disproves the previously suggested existence of linker L2 separating it into two left-handed CCs. The general principles of CC dimer stabilization by disulfide introduction are also discussed.

PubMed: 22119849
DOI: 10.1016/j.jsb.2011.11.014

Experimental method

X-RAY DIFFRACTION (2.3 Å)