5ol9

From Proteopedia

(Difference between revisions)

Current revision

Structure of human mitochondrial transcription elongation factor (TEFM) N-terminal domain

Structural highlights

5ol9 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.302Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Minczuk M, He J, Duch AM, Ettema TJ, Chlebowski A, Dzionek K, Nijtmans LG, Huynen MA, Holt IJ. TEFM (c17orf42) is necessary for transcription of human mtDNA. Nucleic Acids Res. 2011 May;39(10):4284-99. doi: 10.1093/nar/gkq1224. Epub 2011, Jan 28. PMID:21278163 doi:10.1093/nar/gkq1224
↑ Hillen HS, Parshin AV, Agaronyan K, Morozov YI, Graber JJ, Chernev A, Schwinghammer K, Urlaub H, Anikin M, Cramer P, Temiakov D. Mechanism of Transcription Anti-termination in Human Mitochondria. Cell. 2017 Oct 7. pii: S0092-8674(17)31129-7. doi: 10.1016/j.cell.2017.09.035. PMID:29033127 doi:http://dx.doi.org/10.1016/j.cell.2017.09.035

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ol9"

@@ Line 1: / Line 1: @@
 ==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 ==
@@ Line 19: / Line 19: @@
 </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]]

5ol9

From Proteopedia

Current revision

Structure of human mitochondrial transcription elongation factor (TEFM) N-terminal domain

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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