1q89

Crystal structure of the C-domain of the T.vaginalis Inr binding protein, IBP39 (cubic crystal form)

spinqualitylabelsall models 1q89, resolution 2.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1q89 is a 1 chain structure with sequence from Triva. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1q87, 1q88, 1pp7, 1pp8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Transcription start site selection in eukaryotes is mediated through combinations of the TATA, initiator (Inr), and downstream promoter elements (DPE). In Trichomonas vaginalis, a parabasalian flagellate thought to represent an ancient eukaryote lineage, the Inr appears to be solely responsible for start site selection and is recognized by the initiator binding protein 39 kDa (IBP39). IBP39 contains an N-terminal Inr binding domain (IBD) connected via a flexible linker to a C-terminal domain (C domain). Here we present crystal structures of the apoIBD and IBD-Inr complexes and the C domain. The IBD structures reveal a winged-helix motif with prokaryotic and eukaryotic features and a scaffold similar to that of ETS-family proteins. The C domain structure and biochemical studies indicate that it interacts with the T. vaginalis RNAP II large subunit C-terminal domain. These data suggest that binding of IBP39 to the Inr directly recruits RNAP II and in this way initiates transcription. Structural basis of core promoter recognition in a primitive eukaryote.,Schumacher MA, Lau AO, Johnson PJ Cell. 2003 Nov 14;115(4):413-24. PMID:14622596 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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