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[[ | ==X-ray crystal structure of Pyrococcus furiosus transcription elongation factor Spt4/5== | ||
<StructureSection load='3p8b' size='340' side='right' caption='[[3p8b]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3p8b]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P8B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3P8B FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PF0255, Spt4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 Pyrococcus furiosus]), PF1990, Spt5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 Pyrococcus furiosus])</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=3p8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p8b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3p8b RCSB], [http://www.ebi.ac.uk/pdbsum/3p8b PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Spt4/5 in archaea and eukaryote and its bacterial homolog NusG is the only elongation factor conserved in all three domains of life and plays many key roles in cotranscriptional regulation and in recruiting other factors to the elongating RNA polymerase. Here, we present the crystal structure of Spt4/5 as well as the structure of RNA polymerase-Spt4/5 complex using cryoelectron microscopy reconstruction and single particle analysis. The Spt4/5 binds in the middle of RNA polymerase claw and encloses the DNA, reminiscent of the DNA polymerase clamp and ring helicases. The transcription elongation complex model reveals that the Spt4/5 is an upstream DNA holder and contacts the nontemplate DNA in the transcription bubble. These structures reveal that the cellular RNA polymerases also use a strategy of encircling DNA to enhance its processivity as commonly observed for many nucleic acid processing enzymes including DNA polymerases and helicases. | |||
RNA polymerase and transcription elongation factor Spt4/5 complex structure.,Klein BJ, Bose D, Baker KJ, Yusoff ZM, Zhang X, Murakami KS Proc Natl Acad Sci U S A. 2011 Jan 11;108(2):546-50. Epub 2010 Dec 27. PMID:21187417<ref>PMID:21187417</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[RNA polymerase|RNA polymerase]] | *[[RNA polymerase|RNA polymerase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
[[Category: Klein, B J | [[Category: Klein, B J]] | ||
[[Category: Murakami, K S | [[Category: Murakami, K S]] | ||
[[Category: Rna polymerase]] | [[Category: Rna polymerase]] | ||
[[Category: Transcription elongation factor]] | [[Category: Transcription elongation factor]] | ||
[[Category: Transferase-transcription complex]] | [[Category: Transferase-transcription complex]] | ||
Revision as of 15:54, 9 December 2014
X-ray crystal structure of Pyrococcus furiosus transcription elongation factor Spt4/5X-ray crystal structure of Pyrococcus furiosus transcription elongation factor Spt4/5
Structural highlights
Publication Abstract from PubMedSpt4/5 in archaea and eukaryote and its bacterial homolog NusG is the only elongation factor conserved in all three domains of life and plays many key roles in cotranscriptional regulation and in recruiting other factors to the elongating RNA polymerase. Here, we present the crystal structure of Spt4/5 as well as the structure of RNA polymerase-Spt4/5 complex using cryoelectron microscopy reconstruction and single particle analysis. The Spt4/5 binds in the middle of RNA polymerase claw and encloses the DNA, reminiscent of the DNA polymerase clamp and ring helicases. The transcription elongation complex model reveals that the Spt4/5 is an upstream DNA holder and contacts the nontemplate DNA in the transcription bubble. These structures reveal that the cellular RNA polymerases also use a strategy of encircling DNA to enhance its processivity as commonly observed for many nucleic acid processing enzymes including DNA polymerases and helicases. RNA polymerase and transcription elongation factor Spt4/5 complex structure.,Klein BJ, Bose D, Baker KJ, Yusoff ZM, Zhang X, Murakami KS Proc Natl Acad Sci U S A. 2011 Jan 11;108(2):546-50. Epub 2010 Dec 27. PMID:21187417[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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