5O9J

Crystal structure of transcription factor IIB Mja mini-intein

Summary for 5O9J

• Entry DOI: 10.2210/pdb5o9j/pdb
• Descriptor: Transcription initiation factor IIB,Transcription initiation factor IIB, 1,4-DIETHYLENE DIOXIDE, GLYCEROL, ... (6 entities in total)
• Functional Keywords: transcription factor iib, mini-intein, hint fold, hydrolase
• Biological source: Methanocaldococcus jannaschii; More
• Total number of polymer chains: 2
• Total formula weight: 43937.80

Authors

Mikula, K.M.,Iwai, H.,Zhou, D.,Wlodawer, A. (deposition date: 2017-06-19, release date: 2017-11-01, Last modification date: 2024-01-17)

Primary citation

Iwai, H.,Mikula, K.M.,Oeemig, J.S.,Zhou, D.,Li, M.,Wlodawer, A.
Structural Basis for the Persistence of Homing Endonucleases in Transcription Factor IIB Inteins.
J. Mol. Biol., 429:3942-3956, 2017

PubMed Abstract: 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 into the mutualism between the HEN and HINT domains. We propose an evolutionary model of inteins and a functional role of HEN domains in inteins.

PubMed: 29055778
DOI: 10.1016/j.jmb.2017.10.016

Experimental method

X-RAY DIFFRACTION (2 Å)