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{{STRUCTURE_4ejs| PDB=4ejs | SCENE= }}
==Structure of yeast elongator subcomplex Elp456==
===Structure of yeast elongator subcomplex Elp456===
<StructureSection load='4ejs' size='340' side='right' caption='[[4ejs]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
{{ABSTRACT_PUBMED_22556426}}
== Structural highlights ==
<table><tr><td colspan='2'>[[4ejs]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EJS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EJS FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ELP4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c]), ELP5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c]), ELP6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</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=4ejs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ejs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ejs RCSB], [http://www.ebi.ac.uk/pdbsum/4ejs PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Elongator is a multiprotein complex composed of two subcomplexes, Elp1-3 and Elp4-6. Elongator is highly conserved between yeast and humans and plays an important role in RNA polymerase II-mediated transcriptional elongation and many other processes, including cytoskeleton organization, exocytosis, and tRNA modification. Here, we determined the crystal structure of the Elp4-6 subcomplex of yeast. The overall structure of Elp4-6 revealed that Elp6 acts as a bridge to assemble Elp4 and Elp5. Detailed structural and sequence analyses revealed that each subunit in the Elp4-6 subcomplex forms a RecA-ATPase-like fold, although it lacks the key sequence signature of ATPases. Site-directed mutagenesis and biochemical analyses indicated that the Elp4-6 subcomplex can assemble into a hexameric ring-shaped structure in vitro and in vivo. Furthermore, GST pulldown assays showed that the ring-shaped assembly of the Elp4-6 subcomplex is important for its specific histone H3 binding. Our results may shed light on the substrate recognition and assembly of the holo-Elongator complex.


==Function==
Crystal structure of elongator subcomplex Elp4-6.,Lin Z, Zhao W, Diao W, Xie X, Wang Z, Zhang J, Shen Y, Long J J Biol Chem. 2012 Jun 15;287(25):21501-8. Epub 2012 May 2. PMID:22556426<ref>PMID:22556426</ref>
[[http://www.uniprot.org/uniprot/ELP4_YEAST ELP4_YEAST]] Acts as component of the RNA polymerase II elongator complex, which is a major histone acetyltransferase component of the RNA polymerase II (RNAPII) holoenzyme and is involved in transcriptional elongation. Association with elongating RNAPII requires a hyperphosphorylated state of the RNAPII C-terminal domain (CTD). Elongator binds to both naked and nucleosomal DNA, can acetylate both core and nucleosomal histones, and is involved in chromatin remodeling. It acetylates histones H3, preferentially at 'Lys-14', and H4, preferentially at 'Lys-8'. It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin). May also be involved in sensitiviy to Pichia inositovora toxin. May be involved in tRNA modification. ELP4 is required for the complex integrity and the complex HAT activity but is not required for the association of the complex with nascent RNA transcript. Is required for an early step in synthesis of 5-methoxycarbonylmethyl (mcm5) and 5-carbamoylmethyl (ncm5) groups present on uridines at the wobble position in tRNA.<ref>PMID:10024884</ref> <ref>PMID:11296232</ref> <ref>PMID:11689709</ref> <ref>PMID:11904415</ref> <ref>PMID:13680368</ref> <ref>PMID:15138274</ref> <ref>PMID:15769872</ref>  [[http://www.uniprot.org/uniprot/ELP6_YEAST ELP6_YEAST]] Acts as component of the RNA polymerase II elongator complex, which is a major histone acetyltransferase component of the RNA polymerase II (RNAPII) holoenzyme and is involved in transcriptional elongation. Association with elongating RNAPII requires a hyperphosphorylated state of the RNAPII C-terminal domain (CTD). Elongator binds to both naked and nucleosomal DNA, can acetylate both core and nucleosomal histones, and is involved in chromatin remodeling. It acetylates histones H3, preferentially at 'Lys-14', and H4, preferentially at 'Lys-8'. It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin). May also be involved in sensitiviy to Pichia inositovora toxin. May be involved in tRNA modification. ELP6 is required for an early step in synthesis of 5-methoxycarbonylmethyl (mcm5) and 5-carbamoylmethyl (ncm5) groups present on uridines at the wobble position in tRNA.<ref>PMID:10024884</ref> <ref>PMID:11296232</ref> <ref>PMID:11689709</ref> <ref>PMID:11904415</ref> <ref>PMID:13680368</ref> <ref>PMID:15769872</ref>  [[http://www.uniprot.org/uniprot/ELP5_YEAST ELP5_YEAST]] Acts as component of the RNA polymerase II elongator complex, which is a major histone acetyltransferase component of the RNA polymerase II (RNAPII) holoenzyme and is involved in transcriptional elongation. Association with elongating RNAPII requires a hyperphosphorylated state of the RNAPII C-terminal domain (CTD). Elongator binds to both naked and nucleosomal DNA, can acetylate both core and nucleosomal histones, and is involved in chromatin remodeling. It acetylates histones H3, preferentially at 'Lys-14', and H4, preferentially at 'Lys-8'. It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin). May also be involved in sensitiviy to Pichia inositovora toxin. May be involved in tRNA modification. IKI1 is required for an early step in synthesis of 5-methoxycarbonylmethyl (mcm5) and 5-carbamoylmethyl (ncm5) groups present on uridines at the wobble position in tRNA.<ref>PMID:10024884</ref> <ref>PMID:11296232</ref> <ref>PMID:11689709</ref> <ref>PMID:11904415</ref> <ref>PMID:13680368</ref> <ref>PMID:15769872</ref>


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[4ejs]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EJS OCA].
</div>
 
== References ==
==Reference==
<references/>
<references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Saccharomyces cerevisiae s288c]]
[[Category: Saccharomyces cerevisiae s288c]]
[[Category: Lin, Z.]]
[[Category: Lin, Z]]
[[Category: Long, J.]]
[[Category: Long, J]]
[[Category: Shen, Y.]]
[[Category: Shen, Y]]
[[Category: Zhao, W.]]
[[Category: Zhao, W]]
[[Category: Elongator subcomplex elp456]]
[[Category: Elongator subcomplex elp456]]
[[Category: Reca-atpase-like domain fold]]
[[Category: Reca-atpase-like domain fold]]
[[Category: Transcription]]
[[Category: Transcription]]

Revision as of 13:49, 21 December 2014

Structure of yeast elongator subcomplex Elp456Structure of yeast elongator subcomplex Elp456

Structural highlights

4ejs is a 3 chain structure with sequence from Saccharomyces cerevisiae s288c. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:ELP4 (Saccharomyces cerevisiae S288c), ELP5 (Saccharomyces cerevisiae S288c), ELP6 (Saccharomyces cerevisiae S288c)
Resources:FirstGlance, OCA, RCSB, PDBsum

Publication Abstract from PubMed

Elongator is a multiprotein complex composed of two subcomplexes, Elp1-3 and Elp4-6. Elongator is highly conserved between yeast and humans and plays an important role in RNA polymerase II-mediated transcriptional elongation and many other processes, including cytoskeleton organization, exocytosis, and tRNA modification. Here, we determined the crystal structure of the Elp4-6 subcomplex of yeast. The overall structure of Elp4-6 revealed that Elp6 acts as a bridge to assemble Elp4 and Elp5. Detailed structural and sequence analyses revealed that each subunit in the Elp4-6 subcomplex forms a RecA-ATPase-like fold, although it lacks the key sequence signature of ATPases. Site-directed mutagenesis and biochemical analyses indicated that the Elp4-6 subcomplex can assemble into a hexameric ring-shaped structure in vitro and in vivo. Furthermore, GST pulldown assays showed that the ring-shaped assembly of the Elp4-6 subcomplex is important for its specific histone H3 binding. Our results may shed light on the substrate recognition and assembly of the holo-Elongator complex.

Crystal structure of elongator subcomplex Elp4-6.,Lin Z, Zhao W, Diao W, Xie X, Wang Z, Zhang J, Shen Y, Long J J Biol Chem. 2012 Jun 15;287(25):21501-8. Epub 2012 May 2. PMID:22556426[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Lin Z, Zhao W, Diao W, Xie X, Wang Z, Zhang J, Shen Y, Long J. Crystal structure of elongator subcomplex Elp4-6. J Biol Chem. 2012 Jun 15;287(25):21501-8. Epub 2012 May 2. PMID:22556426 doi:http://dx.doi.org/10.1074/jbc.M112.341560

4ejs, resolution 2.61Å

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