3m66

<StructureSection load='3m66' size='340' side='right' caption='[[3m66]], [[Resolution|resolution]] 1.60&Aring;' scene=''>

<table><tr><td colspan='2'>[[3m66]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M66 FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CGI-12, MTERFD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3m66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m66 OCA], [http://pdbe.org/3m66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3m66 RCSB], [http://www.ebi.ac.uk/pdbsum/3m66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3m66 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/MTER1_HUMAN 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).<ref>PMID:17662942</ref>

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== 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<ref>PMID:20430012</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3m66" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Gustafsson, C M]]

[[Category: Hallberg, B M]]

[[Category: Samuelsson, T]]

[[Category: Spahr, H]]

[[Category: Dna binding protein]]

[[Category: Transit peptide]]