3vpy

Publication Abstract from PubMed

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 FHA domain of Arabidopsis Dawdle, determined by multiple-wavelength anomalous dispersion method at 1.7 A resolution. DDL FHA structure displays a seven-stranded beta-sandwich architecture that contains a unique structural motif comprising two long anti-parallel strands. Strikingly, crystal packing of 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. Consistent with the structural observations, co-immuno-precipitation experiments performed in N. benthamiana show that 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 DDL FHA domain as the key molecular event to instate FHA domain-mediated protein-protein interaction in plant miRNA processing.

Crystal Structure of Arabidopsis thaliana Dawdle Forkhead-Associated Domain reveals a conserved phospho-threonine recognition cleft for Dicer-like1 binding.,Machida S, Yuan AY Mol Plant. 2013 Jan 11. PMID:23313986^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.