2eyq: Difference between revisions

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[[Image:2eyq.png|left|200px]]


{{STRUCTURE_2eyq|  PDB=2eyq  |  SCENE=  }}
==Crystal structure of Escherichia coli transcription-repair coupling factor==
 
<StructureSection load='2eyq' size='340' side='right'caption='[[2eyq]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
===Crystal structure of Escherichia coli transcription-repair coupling factor===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2eyq]] is a 2 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=2EYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EYQ FirstGlance]. <br>
{{ABSTRACT_PUBMED_16469698}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2eyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eyq OCA], [https://pdbe.org/2eyq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eyq RCSB], [https://www.ebi.ac.uk/pdbsum/2eyq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eyq ProSAT]</span></td></tr>
[[2eyq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EYQ OCA].  
</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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ey/2eyq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2eyq ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[RapA%2C a Swi2/Snf2 protein|RapA%2C a Swi2/Snf2 protein]]
*[[Transcription-repair coupling factor 3D structures|Transcription-repair coupling factor 3D structures]]
*[[Transcription-repair coupling factor|Transcription-repair coupling factor]]
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:016469698</ref><references group="xtra"/>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Darst, S A.]]
[[Category: Large Structures]]
[[Category: Deaconescu, A M.]]
[[Category: Darst SA]]
[[Category: Hydrolase]]
[[Category: Deaconescu AM]]
[[Category: Mfd]]
[[Category: Sf2 atpase]]

Latest revision as of 12:20, 14 February 2024

Crystal structure of Escherichia coli transcription-repair coupling factorCrystal structure of Escherichia coli transcription-repair coupling factor

Structural highlights

2eyq is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.2Å
Ligands:,
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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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

2eyq, resolution 3.20Å

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