4uzw

High-resolution NMR structures of the domains of Saccharomyces cerevisiae Tho1

spinqualitylabelsall models 4uzw Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4uzw is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function THO1_YEAST Unknown; suppressor of the transcriptional defect of HPR1 by overexpression. Publication Abstract from PubMed THO is a multi-protein complex involved in the formation of messenger ribonuclear particles (mRNPs) by coupling transcription with mRNA processing and export. THO is thought to be formed from five subunits, Tho2p, Hpr1p, Tex1p, Mft1p and Thp2p, and recent work has determined a low-resolution structure of the complex [Poulsen et al. (2014), PLoS One, 9, e103470]. A number of additional proteins are thought to be involved in the formation of mRNP in yeast, including Tho1, which has been shown to bind RNA in vitro and is recruited to actively transcribed chromatin in vivo in a THO-complex and RNA-dependent manner. Tho1 is known to contain a SAP domain at the N-terminus, but the ability to suppress the expression defects of the hpr1Delta mutant of THO was shown to reside in the RNA-binding C-terminal region. In this study, high-resolution structures of both the N-terminal DNA-binding SAP domain and C-terminal RNA-binding domain have been determined. High-resolution NMR structures of the domains of Saccharomyces cerevisiae Tho1.,Jacobsen JO, Allen MD, Freund SM, Bycroft M Acta Crystallogr F Struct Biol Commun. 2016 Jun 1;72(Pt 6):500-6. doi:, 10.1107/S2053230X16007597. Epub 2016 May 23. PMID:27303905 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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