1XTI

Structure of Wildtype human UAP56

Summary for 1XTI

• Entry DOI: 10.2210/pdb1xti/pdb
• Descriptor: Probable ATP-dependent RNA helicase p47, ISOPROPYL ALCOHOL (3 entities in total)
• Functional Keywords: alpha-beta fold, gene regulation
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q13838
• Total number of polymer chains: 1
• Total formula weight: 45309.52

Authors

Shi, H.,Cordin, O.,Minder, C.M.,Linder, P.,Xu, R.M. (deposition date: 2004-10-21, release date: 2004-12-14, Last modification date: 2023-08-23)

Primary citation

Shi, H.,Cordin, O.,Minder, C.M.,Linder, P.,Xu, R.M.
Crystal structure of the human ATP-dependent splicing and export factor UAP56
Proc.Natl.Acad.Sci.Usa, 101:17628-17633, 2004

PubMed Abstract: 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.

PubMed: 15585580
DOI: 10.1073/pnas.0408172101

Experimental method

X-RAY DIFFRACTION (1.95 Å)