1grj

From Proteopedia

(Difference between revisions)

Revision as of 11:27, 28 July 2021

GREA TRANSCRIPT CLEAVAGE FACTOR FROM ESCHERICHIA COLI

Structural highlights

1grj is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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.

Publication Abstract from PubMed

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.

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:7854424^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Stebbins CE, Borukhov S, Orlova M, Polyakov A, Goldfarb A, Darst SA. Crystal structure of the GreA transcript cleavage factor from Escherichia coli. Nature. 1995 Feb 16;373(6515):636-40. PMID:7854424 doi:http://dx.doi.org/10.1038/373636a0

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1grj"

@@ Line 3: / Line 3: @@
 <StructureSection load='1grj' size='340' side='right'caption='[[1grj]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1grj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GRJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1grj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1grj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1grj OCA], [http://pdbe.org/1grj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1grj RCSB], [http://www.ebi.ac.uk/pdbsum/1grj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1grj ProSAT]</span></td></tr>
+</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=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 ==
-[[http://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.
+[[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]]

1grj

From Proteopedia

Revision as of 11:27, 28 July 2021

GREA TRANSCRIPT CLEAVAGE FACTOR FROM ESCHERICHIA COLI

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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