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==X-ray crystal structure of Pyrococcus furiosus transcription elongation factor Spt4/5==
==X-ray crystal structure of Pyrococcus furiosus transcription elongation factor Spt4/5==
<StructureSection load='3p8b' size='340' side='right' caption='[[3p8b]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3p8b' size='340' side='right'caption='[[3p8b]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== 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>
<table><tr><td colspan='2'>[[3p8b]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3p8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p8b OCA], [https://pdbe.org/3p8b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p8b RCSB], [https://www.ebi.ac.uk/pdbsum/3p8b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p8b ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/Q8U440_PYRFU Q8U440_PYRFU]] Stimulates transcription elongation.<ref>PMID:21386817</ref> <ref>PMID:21187417</ref>  [[http://www.uniprot.org/uniprot/Q8TZK1_PYRFU Q8TZK1_PYRFU]] Stimulates transcription elongation.[HAMAP-Rule:MF_00950]<ref>PMID:21187417</ref> <ref>PMID:21386817</ref> 
[https://www.uniprot.org/uniprot/SPT4_PYRFU SPT4_PYRFU] Stimulates transcription elongation.<ref>PMID:21386817</ref> <ref>PMID:21187417</ref>  
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[RNA polymerase|RNA polymerase]]
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
[[Category: Klein, B J]]
[[Category: Klein BJ]]
[[Category: Murakami, K S]]
[[Category: Murakami KS]]
[[Category: Rna polymerase]]
[[Category: Transcription elongation factor]]
[[Category: Transferase-transcription complex]]

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