3m66 | pdb_00003m66
From Proteopedia
Crystal structure of human Mitochondrial Transcription Termination Factor 3
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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 ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn 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
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