1T5I

Crystal structure of the C-terminal domain of UAP56

Summary for 1T5I

• Entry DOI: 10.2210/pdb1t5i/pdb
• Related: 1t6n
• Descriptor: C_TERMINAL DOMAIN OF A PROBABLE ATP-DEPENDENT RNA HELICASE (2 entities in total)
• Functional Keywords: reca-like fold, pre-mrna processing protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q13838
• Total number of polymer chains: 1
• Total formula weight: 20041.70

Authors

Zhao, R.,Green, M.R.,Shen, J. (deposition date: 2004-05-04, release date: 2004-08-31, Last modification date: 2024-02-14)

Primary citation

Zhao, R.,Shen, J.,Green, M.R.,Macmorris, M.,Blumenthal, T.
Crystal structure of UAP56, a "DEXD/H-box" protein involved in pre-mRNA splicing and mRNA export
Structure, 12:1373-1381, 2004

PubMed Abstract: UAP56 is an essential eukaryotic pre-mRNA splicing factor and mRNA export factor. The mechanisms of its functions are not well understood. We determined the crystal structures of the N- and C-terminal domains of human UAP56 (comprising 90% of the full-length UAP56) at 1.9 A resolution. The two domains each have a RecA-like fold and are connected by a flexible linker. The overall fold of each domain is highly similar to the corresponding domains of eIF4A (a prototypic DExD/H-box protein), with differences at the loops and termini. This structural similarity suggests that UAP56 is likely to possess ATPase and helicase activity similar to eIF4A. The NTP binding pocket of UAP56 is occupied by a citrate ion, mimicking the phosphates of NTP and retaining the P loop in an open conformation. The crystal structure of the N-terminal domain of UAP56 also reveals a dimer interface that is potentially important for UAP56's function.

PubMed: 15296731
DOI: 10.1016/j.str.2004.06.006

Experimental method

X-RAY DIFFRACTION (1.9 Å)