Structural highlights
Function
[MTER1_HUMAN] Binds promoter DNA and regulates initiation of transcription. Required for normal mitochondrial transcription, and for normal assembly of mitochondrial respiratory complexes. Required for normal mitochondrial function (By similarity).[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Park CB, Asin-Cayuela J, Camara Y, Shi Y, Pellegrini M, Gaspari M, Wibom R, Hultenby K, Erdjument-Bromage H, Tempst P, Falkenberg M, Gustafsson CM, Larsson NG. MTERF3 is a negative regulator of mammalian mtDNA transcription. Cell. 2007 Jul 27;130(2):273-85. PMID:17662942 doi:10.1016/j.cell.2007.05.046
- ↑ 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
