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spinqualitylabelsall models 1xtk, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

structure of DECD to DEAD mutation of human UAP56

Overview

Pre-mRNA splicing requires the function of a number of RNA-dependent, ATPases/helicases, yet no three-dimensional structure of any spliceosomal, ATPases/helicases is known. The highly conserved DECD-box protein, UAP56/Sub2 is an essential splicing factor that is also important for mRNA, export. The expected ATPase/helicase activity appears to be essential for, the UAP56/Sub2 functions. Here, we show that purified human UAP56 is an, active RNA-dependent ATPase, and we also report the crystal structures of, UAP56 alone and in complex with ADP, as well as a DECD to DEAD mutant. The, structures reveal a unique spatial arrangement of the two conserved, helicase domains, and ADP-binding induces significant conformational, changes of key residues in the ATP-binding pocket. Our structural analyses, suggest a specific protein-RNA displacement model of UAP56/Sub2. The, detailed structural information provides important mechanistic insights, into the splicing function of UAP56/Sub2. The structures also will be, useful for the analysis of other spliceosomal DExD-box ATPases/helicases.

About this Structure

1XTK is a Single protein structure of sequence from Homo sapiens with BME as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the human ATP-dependent splicing and export factor UAP56., Shi H, Cordin O, Minder CM, Linder P, Xu RM, Proc Natl Acad Sci U S A. 2004 Dec 21;101(51):17628-33. Epub 2004 Dec 7. PMID:15585580

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