5o9j
Crystal structure of transcription factor IIB Mja mini-inteinCrystal structure of transcription factor IIB Mja mini-intein
Structural highlights
FunctionTF2B_METJA Stabilizes TBP binding to an archaeal box-A promoter. Also responsible for recruiting RNA polymerase II to the pre-initiation complex (DNA-TBP-TFIIB). Publication Abstract from PubMedInteins 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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