3M66

Crystal structure of human Mitochondrial Transcription Termination Factor 3

Summary for 3M66

• Entry DOI: 10.2210/pdb3m66/pdb
• Descriptor: mTERF domain-containing protein 1, mitochondrial (2 entities in total)
• Functional Keywords: mitochondrion, dna binding protein, transcription factor, transcription termination, transit peptide, transcription
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion: Q96E29
• Total number of polymer chains: 1
• Total formula weight: 31562.94

Authors

Spahr, H.,Samuelsson, T.,Hallberg, B.M.,Gustafsson, C.M. (deposition date: 2010-03-15, release date: 2010-05-05, Last modification date: 2024-02-21)

Primary citation

Spahr, H.,Samuelsson, T.,Hallberg, B.M.,Gustafsson, C.M.
Structure of mitochondrial transcription termination factor 3 reveals a novel nucleic acid-binding domain.
Biochem.Biophys.Res.Commun., 397:386-390, 2010

PubMed Abstract: 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.

PubMed: 20430012
DOI: 10.1016/j.bbrc.2010.04.130

Experimental method

X-RAY DIFFRACTION (1.6 Å)