4dfc: Difference between revisions

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'''Unreleased structure'''


The entry 4dfc is ON HOLD
==Core UvrA/TRCF complex==
<StructureSection load='4dfc' size='340' side='right'caption='[[4dfc]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4dfc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DFC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.803&#8491;</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=4dfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dfc OCA], [https://pdbe.org/4dfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dfc RCSB], [https://www.ebi.ac.uk/pdbsum/4dfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dfc 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>


Authors: Deaconescu, A.M, Grigorieff, N.
==See Also==
 
*[[Transcription-repair coupling factor 3D structures|Transcription-repair coupling factor 3D structures]]
Description: Protein Complex
*[[UvrABC|UvrABC]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Deaconescu AM]]
[[Category: Grigorieff N]]

Latest revision as of 17:34, 14 March 2024

Core UvrA/TRCF complexCore UvrA/TRCF complex

Structural highlights

4dfc is a 4 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.803Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3] [4] [5]

See Also

References

  1. ↑ Selby CP, Sancar A. Molecular mechanism of transcription-repair coupling. Science. 1993 Apr 2;260(5104):53-8. PMID:8465200
  2. ↑ Selby CP, Sancar A. Structure and function of transcription-repair coupling factor. I. Structural domains and binding properties. J Biol Chem. 1995 Mar 3;270(9):4882-9. PMID:7876261
  3. ↑ Selby CP, Sancar A. Structure and function of transcription-repair coupling factor. II. Catalytic properties. J Biol Chem. 1995 Mar 3;270(9):4890-5. PMID:7876262
  4. ↑ Park JS, Marr MT, Roberts JW. E. coli Transcription repair coupling factor (Mfd protein) rescues arrested complexes by promoting forward translocation. Cell. 2002 Jun 14;109(6):757-67. PMID:12086674
  5. ↑ Murphy MN, Gong P, Ralto K, Manelyte L, Savery NJ, Theis K. An N-terminal clamp restrains the motor domains of the bacterial transcription-repair coupling factor Mfd. Nucleic Acids Res. 2009 Oct;37(18):6042-53. Epub 2009 Aug 21. PMID:19700770 doi:10.1093/nar/gkp680

4dfc, resolution 2.80Å

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