1grj: Difference between revisions

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 ==GREA TRANSCRIPT CLEAVAGE FACTOR FROM ESCHERICHIA COLI==
-<StructureSection load='1grj' size='340' side='right' caption='[[1grj]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<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/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>
-</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='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>
+<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]]
@@ Line 18: / Line 19: @@
 </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>
-<div style="background-color:#fffaf0;">
-== 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<ref>PMID:7854424</ref>
+==See Also==
+*[[Elongation factor 3D structures|Elongation factor 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1grj" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
-[[Category: Darst, S A]]
+[[Category: Large Structures]]
-[[Category: Stebbins, C E]]
+[[Category: Darst SA]]
-[[Category: Transcript cleavage factor]]
+[[Category: Stebbins CE]]
-[[Category: Transcript elongation factor]]
-[[Category: Transcription regulation]]