1grj: Difference between revisions

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[[Image:1grj.jpg|left|200px]]


{{Structure
==GREA TRANSCRIPT CLEAVAGE FACTOR FROM ESCHERICHIA COLI==
|PDB= 1grj |SIZE=350|CAPTION= <scene name='initialview01'>1grj</scene>, resolution 2.2&Aring;
<StructureSection load='1grj' size='340' side='right'caption='[[1grj]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1grj]] is a 1 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=1GRJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GRJ FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1grj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1grj OCA], [https://pdbe.org/1grj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1grj RCSB], [https://www.ebi.ac.uk/pdbsum/1grj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1grj ProSAT]</span></td></tr>
}}
</table>
== Function ==
[https://www.uniprot.org/uniprot/GREA_ECOLI GREA_ECOLI] Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides.
== 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/gr/1grj_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=1grj ConSurf].
<div style="clear:both"></div>


'''GREA TRANSCRIPT CLEAVAGE FACTOR FROM ESCHERICHIA COLI'''
==See Also==
 
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Transcription elongation factors stimulate the activity of DNA-dependent RNA polymerases by increasing the overall elongation rate and the completion of RNA chains. One group of such factors, which includes Escherichia coli GreA, GreB and eukaryotic SII (TFIIS), acts by inducing hydrolytic cleavage of the transcript within the RNA polymerase, followed by release of the 3'-terminal fragment. Here we report the crystal structure of GreA at 2.2 A resolution. The structure contains an amino-terminal domain consisting of an antiparallel alpha-helical coiled-coil dimer which extends into solution, reminiscent of the coiled coil in seryl-tRNA synthetases. A site near the tip of the coiled-coil 'finger' plays a direct role in the transcript cleavage reaction by contacting the 3'-end of the transcript. The structure exhibits an unusual asymmetric charge distribution which indicates the manner in which GreA interacts with the RNA polymerase elongation complex.
 
==About this Structure==
1GRJ is a [[Single protein]] structure of 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=1GRJ OCA].
 
==Reference==
Crystal structure of the GreA transcript cleavage factor from Escherichia coli., Stebbins CE, Borukhov S, Orlova M, Polyakov A, Goldfarb A, Darst SA, Nature. 1995 Feb 16;373(6515):636-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7854424 7854424]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Darst, S A.]]
[[Category: Darst SA]]
[[Category: Stebbins, C E.]]
[[Category: Stebbins CE]]
[[Category: transcript cleavage factor]]
[[Category: transcript elongation factor]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:26:57 2008''

Latest revision as of 10:26, 7 February 2024

GREA TRANSCRIPT CLEAVAGE FACTOR FROM ESCHERICHIA COLIGREA TRANSCRIPT CLEAVAGE FACTOR FROM ESCHERICHIA COLI

Structural highlights

1grj is a 1 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 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GREA_ECOLI Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides.

Evolutionary Conservation

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

See Also

1grj, resolution 2.20Å

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