5o20

Structure of Nrd1 RNA binding domain in complex with RNA (UUAGUAAUCC)

spinqualitylabelsall models 5o20, resolution 3.53Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5o20 is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.53Å Ligands: TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NRD1_YEAST Plays a role in sequence-specific regulation of nuclear pre-mRNA abundance. Publication Abstract from PubMed Transcription termination of non-coding RNAs is regulated in yeast by a complex of three RNA binding proteins: Nrd1, Nab3 and Sen1. Nrd1 is central in this process by interacting with Rbp1 of RNA polymerase II, Trf4 of TRAMP and GUAA/G terminator sequences. We lack structural data for the last of these binding events. We determined the structures of Nrd1 RNA binding domain and its complexes with three GUAA-containing RNAs, characterized RNA binding energetics and tested rationally designed mutants in vivo. The Nrd1 structure shows an RRM domain fused with a second alpha/beta domain that we name split domain (SD), because it is formed by two non-consecutive segments at each side of the RRM. The GUAA interacts with both domains and with a pocket of water molecules, trapped between the two stacking adenines and the SD. Comprehensive binding studies demonstrate for the first time that Nrd1 has a slight preference for GUAA over GUAG and genetic and functional studies suggest that Nrd1 RNA binding domain might play further roles in non-coding RNAs transcription termination. The structure of transcription termination factor Nrd1 reveals an original mode for GUAA recognition.,Franco-Echevarria E, Gonzalez-Polo N, Zorrilla S, Martinez-Lumbreras S, Santiveri CM, Campos-Olivas R, Sanchez M, Calvo O, Gonzalez B, Perez-Canadillas JM Nucleic Acids Res. 2017 Sep 29;45(17):10293-10305. doi: 10.1093/nar/gkx685. PMID:28973465 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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