5ol9: Difference between revisions

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 ==Structure of human mitochondrial transcription elongation factor (TEFM) N-terminal domain==
-<StructureSection load='5ol9' size='340' side='right' caption='[[5ol9]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
+<StructureSection load='5ol9' size='340' side='right'caption='[[5ol9]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ol9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OL9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OL9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ol9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OL9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OL9 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.302&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ol8|5ol8]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></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=5ol9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ol9 OCA], [http://pdbe.org/5ol9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ol9 RCSB], [http://www.ebi.ac.uk/pdbsum/5ol9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ol9 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ol9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ol9 OCA], [https://pdbe.org/5ol9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ol9 RCSB], [https://www.ebi.ac.uk/pdbsum/5ol9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ol9 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TEFM_HUMAN TEFM_HUMAN]] Transcription elongation factor which increases mitochondrial RNA polymerase processivity. Regulates transcription of the mitochondrial genome, including genes important for the oxidative phosphorylation machinery.<ref>PMID:21278163</ref>
+[https://www.uniprot.org/uniprot/TEFM_HUMAN TEFM_HUMAN] Transcription elongation factor which increases mitochondrial RNA polymerase processivity. Regulates transcription of the mitochondrial genome, including genes important for the oxidative phosphorylation machinery.<ref>PMID:21278163</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+In human mitochondria, transcription termination events at a G-quadruplex region near the replication origin are thought to drive replication of mtDNA by generation of an RNA primer. This process is suppressed by a key regulator of mtDNA-the transcription factor TEFM. We determined the structure of an anti-termination complex in which TEFM is bound to transcribing mtRNAP. The structure reveals interactions of the dimeric pseudonuclease core of TEFM with mobile structural elements in mtRNAP and the nucleic acid components of the elongation complex (EC). Binding of TEFM to the DNA forms a downstream "sliding clamp," providing high processivity to the EC. TEFM also binds near the RNA exit channel to prevent formation of the RNA G-quadruplex structure required for termination and thus synthesis of the replication primer. Our data provide insights into target specificity of TEFM and mechanisms by which it regulates the switch between transcription and replication of mtDNA.
+Mechanism of Transcription Anti-termination in Human Mitochondria.,Hillen HS, Parshin AV, Agaronyan K, Morozov YI, Graber JJ, Chernev A, Schwinghammer K, Urlaub H, Anikin M, Cramer P, Temiakov D Cell. 2017 Oct 7. pii: S0092-8674(17)31129-7. doi: 10.1016/j.cell.2017.09.035. PMID:29033127<ref>PMID:29033127</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5ol9" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Elongation factor 3D structures|Elongation factor 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Agaronyan, K]]
+[[Category: Homo sapiens]]
-[[Category: Anikin, M]]
+[[Category: Large Structures]]
-[[Category: Chernev, A]]
+[[Category: Agaronyan K]]
-[[Category: Cramer, P]]
+[[Category: Anikin M]]
-[[Category: Graber, J J]]
+[[Category: Chernev A]]
-[[Category: Hillen, H S]]
+[[Category: Cramer P]]
-[[Category: Morozov, Y]]
+[[Category: Graber JJ]]
-[[Category: Parshin, A V]]
+[[Category: Hillen HS]]
-[[Category: Schwinghammer, K]]
+[[Category: Morozov Y]]
-[[Category: Temiakov, D]]
+[[Category: Parshin AV]]
-[[Category: Urlaub, H]]
+[[Category: Schwinghammer K]]
-[[Category: Elongation factor]]
+[[Category: Temiakov D]]
-[[Category: Mitochondria]]
+[[Category: Urlaub H]]
-[[Category: Resolvase]]
-[[Category: Rna polymerase]]
-[[Category: Transcription]]