Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
In mammalian cells, a family of mitochondrial transcription termination factors (MTERFs) regulates mitochondrial gene expression. MTERF family members share a approximately 270 residues long MTERF-domain required for DNA binding and transcription regulation. However, the structure of this widely conserved domain is unknown. Here, we show that the MTERF-domain of human MTERF3 forms a half-doughnut-shaped right-handed superhelix. The superhelix is built from alpha-helical tandem repeats that display a novel triangular three-helix motif. This repeat motif, which we denote the MTERF-motif, is a conserved structural element present in proteins from metazoans, plants, and protozoans. Furthermore, a narrow, strongly positively charged nucleic acid-binding path is found in the middle of the concave side of the half-doughnut. This arrangement suggests a half clamp nucleic acid-binding mode for MTERF-domains.
Structure of mitochondrial transcription termination factor 3 reveals a novel nucleic acid-binding domain.,Spahr H, Samuelsson T, Hallberg BM, Gustafsson CM Biochem Biophys Res Commun. 2010 Jul 2;397(3):386-90. Epub 2010 Apr 27. PMID:20430012[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Spahr H, Samuelsson T, Hallberg BM, Gustafsson CM. Structure of mitochondrial transcription termination factor 3 reveals a novel nucleic acid-binding domain. Biochem Biophys Res Commun. 2010 Jul 2;397(3):386-90. Epub 2010 Apr 27. PMID:20430012 doi:10.1016/j.bbrc.2010.04.130
