View source for 3lpe

==Crystal structure of Spt4/5NGN heterodimer complex from Methanococcus jannaschii==
<StructureSection load='3lpe' size='340' side='right' caption='[[3lpe]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3lpe]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LPE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LPE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ewg|3ewg]], [[1ryq|1ryq]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MJ0372 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii]), rpoE2, MJ0396 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] </span></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=3lpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lpe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lpe RCSB], [http://www.ebi.ac.uk/pdbsum/3lpe PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/NUSG_METJA NUSG_METJA]] Stimulates transcription elongation.<ref>PMID:20197319</ref>  [[http://www.uniprot.org/uniprot/RPOE2_METJA RPOE2_METJA]] Stimulates transcription elongation.<ref>PMID:20197319</ref>  
== 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/lp/3lpe_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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Spt5 is the only known RNA polymerase-associated factor that is conserved in all three domains of life. We have solved the structure of the Methanococcus jannaschii Spt4/5 complex by X-ray crystallography, and characterized its function and interaction with the archaeal RNAP in a wholly recombinant in vitro transcription system. Archaeal Spt4 and Spt5 form a stable complex that associates with RNAP independently of the DNA-RNA scaffold of the elongation complex. The association of Spt4/5 with RNAP results in a stimulation of transcription processivity, both in the absence and the presence of the non-template strand. A domain deletion analysis reveals the molecular anatomy of Spt4/5--the Spt5 Nus-G N-terminal (NGN) domain is the effector domain of the complex that both mediates the interaction with RNAP and is essential for its elongation activity. Using a mutagenesis approach, we have identified a hydrophobic pocket on the Spt5 NGN domain as binding site for RNAP, and reciprocally the RNAP clamp coiled-coil motif as binding site for Spt4/5.

Spt4/5 stimulates transcription elongation through the RNA polymerase clamp coiled-coil motif.,Hirtreiter A, Damsma GE, Cheung AC, Klose D, Grohmann D, Vojnic E, Martin AC, Cramer P, Werner F Nucleic Acids Res. 2010 Jul 1;38(12):4040-51. Epub 2010 Mar 2. PMID:20197319<ref>PMID:20197319</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>

==See Also==
*[[RNA polymerase|RNA polymerase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: DNA-directed RNA polymerase]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Cheung, A C.M]]
[[Category: Cramer, P]]
[[Category: Damsma, G E]]
[[Category: Grohmann, D]]
[[Category: Hirtreiter, A]]
[[Category: Klose, D]]
[[Category: Martin, A C.R]]
[[Category: Vojnic, E]]
[[Category: Werner, F]]
[[Category: Archaea]]
[[Category: Dna-directed rna polymerase]]
[[Category: Evolution]]
[[Category: Metal-binding]]
[[Category: Nucleotidyltransferase]]
[[Category: Nusg]]
[[Category: Spt4]]
[[Category: Spt5]]
[[Category: Transcription]]
[[Category: Transcription regulation]]
[[Category: Transferase]]
[[Category: Zinc-finger]]