1t6n

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Revision as of 17:15, 12 November 2007

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spinqualitylabelsall models 1t6n, resolution 1.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of the N-terminal domain of human UAP56

Overview

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.

About this Structure

1T6N is a Single protein structure of sequence from Homo sapiens with FLC as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of UAP56, a DExD/H-box protein involved in pre-mRNA splicing and mRNA export., Zhao R, Shen J, Green MR, MacMorris M, Blumenthal T, Structure. 2004 Aug;12(8):1373-81. PMID:15296731

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