6xeo
From Proteopedia
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			|  (New page: '''Unreleased structure'''  The entry 6xeo is ON HOLD  until Paper Publication  Authors: Brugger, C., Deaconescu, A.  Description: Structure of Mfd bound to dsDNA [[Category: Unreleased St...) | |||
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Mfd bound to dsDNA== | |
| + | <StructureSection load='6xeo' size='340' side='right'caption='[[6xeo]], [[Resolution|resolution]] 5.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6xeo]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XEO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XEO 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]] 5.5Å</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=6xeo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xeo OCA], [https://pdbe.org/6xeo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xeo RCSB], [https://www.ebi.ac.uk/pdbsum/6xeo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xeo 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== | |
| - | + | *[[Transcription-repair coupling factor 3D structures|Transcription-repair coupling factor 3D structures]] | |
| - | + | == References == | |
| - | [[Category:  | + | <references/> | 
| - | [[Category: Brugger | + | __TOC__ | 
| - | [[Category: Deaconescu | + | </StructureSection> | 
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Brugger C]] | ||
| + | [[Category: Deaconescu A]] | ||
Current revision
Structure of Mfd bound to dsDNA
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