3VPY

Crystal structure of Arabidopsis DDL FHA domain

3VPY の概要

• エントリーDOI: 10.2210/pdb3vpy/pdb
• 分子名称: FHA domain-containing protein DDL (2 entities in total)
• 機能のキーワード: fha domain, dcl1 pt recognition, arabidopsis dcl1, protein binding
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• 細胞内の位置: Nucleus: Q8W4D8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17530.13

構造登録者

Yuan, Y.A.,Machida, S. (登録日: 2012-03-15, 公開日: 2013-02-06, 最終更新日: 2024-10-16)

主引用文献

Machida, S.,Yuan, A.Y.
Crystal Structure of Arabidopsis thaliana Dawdle Forkhead-Associated Domain reveals a conserved phospho-threonine recognition cleft for Dicer-like1 binding.
Mol Plant, 2013

PubMed Abstract: Dawdle (DDL) is a microRNA processing protein essential for the development of Arabidopsis. DDL contains a putative nuclear localization signal at its amino-terminus and forkhead-associated (FHA) domain at the carboxyl-terminus. Here, we report the crystal structure of the FHA domain of Arabidopsis Dawdle, determined by multiple-wavelength anomalous dispersion method at 1.7-Å resolution. DDL FHA structure displays a seven-stranded β-sandwich architecture that contains a unique structural motif comprising two long anti-parallel strands. Strikingly, crystal packing of the DDL FHA domain reveals that a glutamate residue from the symmetry-related DDL FHA domain, a structural mimic of the phospho-threonine, is specifically recognized by the structurally conserved phospho-threonine binding cleft. Consistently with the structural observations, co-immuno-precipitation experiments performed in Nicotiana benthamiana show that the DDL FHA domain co-immuno-precipitates with DCL1 fragments containing the predicted pThr+3(Ile/Val/Leu/Asp) motif. Taken together, we count the recognition of the target residue by the canonical binding cleft of the DDL FHA domain as the key molecular event to instate FHA domain-mediated protein-protein interaction in plant miRNA processing.

PubMed: 23313986
DOI: 10.1093/mp/sst007

実験手法

X-RAY DIFFRACTION (1.7 Å)