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. Author manuscript; available in PMC: 2013 Sep 1.
Published in final edited form as: Biochim Biophys Acta. 2011 Nov 25;1819(9-10):939–947. doi: 10.1016/j.bbagrm.2011.11.004

Figure 2. The X-ray Crystallographic Structure of the Mitochondrial Transcription Termination Factor MTERF1 Bound to the tRNALeu Mitochondrial DNA Termination Sequence.

Figure 2

MTERF1 utilizes a unique DNA binding mode that results in duplex unwinding and eversion of three nucleotide bases. MTERF1 is shown in green with its molecular surface shown in transparent grey; the DNA termination site is shown in orange; everted bases are shown as yellow sticks. Inset: π-stacking interactions with the MTERF1 residues (dark green, purple, and blue) stabilize the three corresponding DNA bases (yellow) in an extrahelical position. These interactions are essential for termination activity.