5o9i | pdb_00005o9i

Crystal structure of transcription factor IIB Mvu mini-intein

spinqualitylabelsall models 5o9i, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5o9i is a 2 chain structure with sequence from Methanocaldococcus vulcanius M7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C9REA0_METVM Stabilizes TBP binding to an archaeal box-A promoter. Also responsible for recruiting RNA polymerase II to the pre-initiation complex (DNA-TBP-TFIIB).[HAMAP-Rule:MF_00383] Publication Abstract from PubMed Inteins are mobile genetic elements that are spliced out of proteins after translation. Some inteins contain a homing endonuclease (HEN) responsible for their propagation. Hedgehog/INTein (HINT) domains catalyzing protein splicing and their nested HEN domains are thought to be functionally independent because of the existence of functional mini-inteins without HEN domains. Despite the lack of obvious mutualism between HEN and HINT domains, HEN domains are persistently found at one specific site in inteins, indicating their potential functional role in protein splicing. Here we report crystal structures of inactive and active mini-inteins derived from inteins residing in the transcription factor IIB of Methanococcus jannaschii and Methanocaldococcus vulcanius, revealing a novel modified HINT fold that might provide new insights on the mutualism between the HEN and HINT domains. We propose an evolutionary model of inteins and a functional role of HEN domains in inteins. Structural basis for the persistence of homing endonucleases in transcription factor IIB inteins.,Iwai H, Mikula KM, Oeemig JS, Zhou D, Li M, Wlodawer A J Mol Biol. 2017 Oct 18. pii: S0022-2836(17)30498-9. doi:, 10.1016/j.jmb.2017.10.016. PMID:29055778 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transcription initiation factors 3D structures

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