1UX5

Crystal Structures of a Formin Homology-2 domain reveal a flexibly tethered dimer architecture

1UX5 の概要

• エントリーDOI: 10.2210/pdb1ux5/pdb
• 関連するPDBエントリー: 1UX4
• 分子名称: BNI1 PROTEIN (2 entities in total)
• 機能のキーワード: structural protein, fh2 actin cytoskeleton
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47395.86

構造登録者

Xu, Y.,Moseley, J.B.,Sagot, I.,Poy, F.,Pellman, D.,Goode, B.L.,Eck, M.J. (登録日: 2004-02-19, 公開日: 2004-03-11, 最終更新日: 2024-10-23)

主引用文献

Xu, Y.,Moseley, J.B.,Sagot, I.,Poy, F.,Pellman, D.,Goode, B.L.,Eck, M.J.
Crystal Structures of a Formin Homology-2 Domain Reveal a Tethered Dimer Architecture
Cell(Cambridge,Mass.), 116:711-, 2004

PubMed Abstract: Formin proteins participate in a wide range of cytoskeletal processes in all eukaryotes. The defining feature of formins is a highly conserved approximately 400 residue region, the Formin Homology-2 (FH2) domain, which has recently been found to nucleate actin filaments. Here we report crystal structures of the S. cerevesiae Bni1p FH2 domain. The mostly alpha-helical FH2 domain forms a unique "tethered dimer" in which two elongated actin binding heads are tied together at either end by an unusual lasso and linker structure. Biochemical and crystallographic observations indicate that the dimer is stable but flexible, with flexibility between the two halves of the dimer conferred by the linker segments. Although each half of the dimer is competent to interact with filament ends, the intact dimer is required for actin nucleation and processive capping. The tethered dimer architecture may allow formins to stair-step on the barbed end of an elongating nascent filament.

PubMed: 15006353
DOI: 10.1016/S0092-8674(04)00210-7

実験手法

X-RAY DIFFRACTION (2.5 Å)