4UZX
High-resolution NMR structures of the domains of Saccharomyces cerevisiae Tho1
Summary for 4UZX
| Entry DOI | 10.2210/pdb4uzx/pdb |
| Related | 4UZM 4UZW |
| NMR Information | BMRB: 25214 |
| Descriptor | PROTEIN THO1 (1 entity in total) |
| Functional Keywords | rna binding protein, tho1 |
| Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) |
| Total number of polymer chains | 1 |
| Total formula weight | 7501.49 |
| Authors | Jacobsen, J.O.B.,Allen, M.D.,Freund, S.M.V.,Bycroft, M. (deposition date: 2014-09-09, release date: 2014-12-17, Last modification date: 2024-05-15) |
| Primary citation | Jacobsen, J.O.B.,Allen, M.D.,Freund, S.M.V.,Bycroft, M. High-Resolution NMR Structures of the Domains of Saccharomyces Cerevisiae Tho1. Acta Crystallogr.,Sect.F, 72:500-, 2016 Cited by PubMed Abstract: 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 hpr1Δ 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. PubMed: 27303905DOI: 10.1107/S2053230X16007597 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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