View source for 6eqy


==4th KOW domain of human hSpt5==
<StructureSection load='6eqy' size='340' side='right'caption='[[6eqy]], [[NMR_Ensembles_of_Models | 14 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6eqy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EQY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EQY FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SUPT5H, SPT5, SPT5H ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6eqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eqy OCA], [http://pdbe.org/6eqy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eqy RCSB], [http://www.ebi.ac.uk/pdbsum/6eqy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eqy ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/SPT5H_HUMAN SPT5H_HUMAN]] Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites. DSIF can also positively regulate transcriptional elongation and is required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences.<ref>PMID:9450929</ref> <ref>PMID:9514752</ref> <ref>PMID:9857195</ref> <ref>PMID:10199401</ref> <ref>PMID:10393184</ref> <ref>PMID:10421630</ref> <ref>PMID:10075709</ref> <ref>PMID:10454543</ref> <ref>PMID:10912001</ref> <ref>PMID:10757782</ref> <ref>PMID:11112772</ref> <ref>PMID:11553615</ref> <ref>PMID:11809800</ref> <ref>PMID:12653964</ref> <ref>PMID:12718890</ref> <ref>PMID:15380072</ref> <ref>PMID:14701750</ref> <ref>PMID:15136722</ref> <ref>PMID:16214896</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The human transcription elongation factor DSIF is highly conserved throughout all kingdoms of life and plays multiple roles during transcription. DSIF is a heterodimer, consisting of Spt4 and Spt5 that interacts with RNA polymerase II (RNAP II). DSIF binds to the elongation complex and induces promoter-proximal pausing of RNAP II. Human Spt5 consists of a NusG N-terminal (NGN) domain motif, which is followed by several KOW domains. We determined the solution structures of the human Spt5 KOW4 and the C-terminal domain by nuclear magnetic resonance spectroscopy. In addition to the typical KOW fold, the solution structure of KOW4 revealed an N-terminal four-stranded beta-sheet, previously designated as the KOW3-KOW4 linker. In solution, the C-terminus of Spt5 consists of two beta-barrel folds typical for KOW domains, designated KOW6 and KOW7. We also analysed the nucleic acid and RNAP II binding properties of the KOW domains. KOW4 variants interacted with nucleic acids, preferentially single stranded RNA, whereas no nucleic acid binding could be detected for KOW6-7. Weak binding of KOW4 to the RNAP II stalk, which is comprised of Rpb4/7, was also detected, consistent with transient interactions between Spt5 and these RNAP II subunits.

Structure and nucleic acid binding properties of KOW domains 4 and 6-7 of human transcription elongation factor DSIF.,Zuber PK, Hahn L, Reinl A, Schweimer K, Knauer SH, Gottesman ME, Rosch P, Wohrl BM Sci Rep. 2018 Aug 3;8(1):11660. doi: 10.1038/s41598-018-30042-3. PMID:30076330<ref>PMID:30076330</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6eqy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Roesch, P]]
[[Category: Schweimer, K]]
[[Category: Woehrl, B M]]
[[Category: Zuber, P K]]
[[Category: Dsif. transcription elongation]]
[[Category: Transcription]]