1pp7
From Proteopedia
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Crystal structure of the T. vaginalis Initiator binding protein bound to the ferredoxin Inr
Overview
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.
About this Structure
1PP7 is a Single protein structure of sequence from Trichomonas vaginalis with ZN as ligand. Full crystallographic information is available from OCA.
Reference
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
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