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6x2f
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Mfd-bound E.coli RNA polymerase elongation complex - L2 state== | |
| + | <StructureSection load='6x2f' size='340' side='right'caption='[[6x2f]], [[Resolution|resolution]] 4.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6x2f]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6X2F FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6x2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x2f OCA], [https://pdbe.org/6x2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x2f RCSB], [https://www.ebi.ac.uk/pdbsum/6x2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x2f ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MFD_ECOLI MFD_ECOLI] Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site. Can also dissociate RNAP that is blocked by low concentration of nucleoside triphosphates or by physical obstruction, such as bound proteins. In addition, can rescue arrested complexes by promoting forward translocation. Has ATPase activity, which is required for removal of stalled RNAP, but seems to lack helicase activity. May act through a translocase activity that rewinds upstream DNA, leading either to translocation or to release of RNAP when the enzyme active site can not continue elongation.<ref>PMID:8465200</ref> <ref>PMID:7876261</ref> <ref>PMID:7876262</ref> <ref>PMID:12086674</ref> <ref>PMID:19700770</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | |
| - | + | *[[Transcription-repair coupling factor 3D structures|Transcription-repair coupling factor 3D structures]] | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chen J]] | ||
| + | [[Category: Darst SA]] | ||
| + | [[Category: Kang JY]] | ||
| + | [[Category: Llewellyn E]] | ||
Current revision
Mfd-bound E.coli RNA polymerase elongation complex - L2 state
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