5WHF

Crystal structure of vimentin coil 1B packed in a high-order filamentous form

5WHF の概要

• エントリーDOI: 10.2210/pdb5whf/pdb
• 分子名称: Vimentin, GLYCEROL (3 entities in total)
• 機能のキーワード: intermediate filament, oligomerization, coiled coil, helical domain, structural protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 86661.66

構造登録者

Obiero, J.M.,Pang, A.H.,Tsodikov, O.V. (登録日: 2017-07-16, 公開日: 2018-06-20, 最終更新日: 2023-10-04)

主引用文献

Pang, A.H.,Obiero, J.M.,Kulczyk, A.W.,Sviripa, V.M.,Tsodikov, O.V.
A crystal structure of coil 1B of vimentin in the filamentous form provides a model of a high-order assembly of a vimentin filament.
FEBS J., 285:2888-2899, 2018

PubMed Abstract: Vimentin is an intermediate filament (IF) protein that is expressed in leukocytes, fibroblasts and endothelial cells of blood vessels. Vimentin filaments contribute to structural stability of the cell membrane, organelle positioning and protein transport. Vimentin self-assembles into a dimer that subsequently forms high-order structures, including tetramers and octamers. The details of IF assembly at crystallographic resolutions are limited to the tetrameric form. We describe a crystal structure of a fragment of a vimentin rod domain (coil 1B) with a dimer of tetramers in the asymmetric unit. Coil 1B in the crystal is in an infinitely high-order filamentous assembly state, in which the tetramers are packed against each other laterally in an antiparallel fashion across the crystal lattice. In one of the directions of lateral packing, the tetramers pack against each other strictly head-to-tail, and in the orthogonal direction the tetramers pack in a staggered manner. This organization of the tetramers of coil 1B in the crystal lattice, together with previously reported biochemical and structural data, yield a model of high-order vimentin filament assembly.

PubMed: 29905014
DOI: 10.1111/febs.14585

実験手法

X-RAY DIFFRACTION (2.25 Å)