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4h3k

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Revision as of 22:55, 24 December 2014

Crystal structure of a ternary complex of human symplekin NTD, human Ssu72 and a RNA polymerase II CTD peptide phosphorylated at Ser-2, Ser-5 and Ser-7

Structural highlights

4h3k is a 5 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	3o2q, 4h3h
Gene:	SYMPK, SPK (HUMAN), SSU72, HSPC182, PNAS-120 (HUMAN)
Activity:	Phosphoprotein phosphatase, with EC number 3.1.3.16
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[SYMPK_HUMAN] Scaffold protein that functions as a component of a multimolecular complex involved in histone mRNA 3'-end processing. Specific component of the tight junction (TJ) plaque, but might not be an exclusively junctional component. May have a house-keeping rule. Is involved in pre-mRNA polyadenylation. Enhances SSU72 phosphatase activity.^[1] ^[2] [SSU72_HUMAN] Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination. Plays a role in pre-mRNA polyadenylation via its interaction with SYMPK.^[3] ^[4] ^[5]

Publication Abstract from PubMed

Ssu72, an RNA polymerase II C-terminal domain (CTD) phospho-Ser5 (pSer5) phosphatase, was recently reported to have pSer7 phosphatase activity as well. We report here the crystal structure of a ternary complex of the N-terminal domain of human symplekin, human Ssu72, and a 10-mer pSer7 CTD peptide. Surprisingly, the peptide is bound in the Ssu72 active site with its backbone running in the opposite direction compared with a pSer5 peptide. The pSer7 phosphatase activity of Ssu72 is approximately 4000-fold lower than its pSer5 phosphatase activity toward a peptide substrate, consistent with the structural observations.

An unexpected binding mode for a Pol II CTD peptide phosphorylated at Ser7 in the active site of the CTD phosphatase Ssu72.,Xiang K, Manley JL, Tong L Genes Dev. 2012 Oct 15;26(20):2265-70. doi: 10.1101/gad.198853.112. PMID:23070812^[6]

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

References

↑ Kolev NG, Steitz JA. Symplekin and multiple other polyadenylation factors participate in 3'-end maturation of histone mRNAs. Genes Dev. 2005 Nov 1;19(21):2583-92. Epub 2005 Oct 17. PMID:16230528 doi:10.1101/gad.1371105
↑ Xiang K, Nagaike T, Xiang S, Kilic T, Beh MM, Manley JL, Tong L. Crystal structure of the human symplekin-Ssu72-CTD phosphopeptide complex. Nature. 2010 Sep 22. PMID:20861839 doi:10.1038/nature09391
↑ St-Pierre B, Liu X, Kha LC, Zhu X, Ryan O, Jiang Z, Zacksenhaus E. Conserved and specific functions of mammalian ssu72. Nucleic Acids Res. 2005 Jan 19;33(2):464-77. Print 2005. PMID:15659578 doi:http://dx.doi.org/33/2/464
↑ Xiang K, Nagaike T, Xiang S, Kilic T, Beh MM, Manley JL, Tong L. Crystal structure of the human symplekin-Ssu72-CTD phosphopeptide complex. Nature. 2010 Sep 22. PMID:20861839 doi:10.1038/nature09391
↑ Xiang K, Manley JL, Tong L. An unexpected binding mode for a Pol II CTD peptide phosphorylated at Ser7 in the active site of the CTD phosphatase Ssu72. Genes Dev. 2012 Oct 15;26(20):2265-70. doi: 10.1101/gad.198853.112. PMID:23070812 doi:http://dx.doi.org/10.1101/gad.198853.112
↑ Xiang K, Manley JL, Tong L. An unexpected binding mode for a Pol II CTD peptide phosphorylated at Ser7 in the active site of the CTD phosphatase Ssu72. Genes Dev. 2012 Oct 15;26(20):2265-70. doi: 10.1101/gad.198853.112. PMID:23070812 doi:http://dx.doi.org/10.1101/gad.198853.112

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4h3k"

@@ Line 10: / Line 10: @@
 <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=4h3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h3k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h3k RCSB], [http://www.ebi.ac.uk/pdbsum/4h3k PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/SYMPK_HUMAN SYMPK_HUMAN]] Scaffold protein that functions as a component of a multimolecular complex involved in histone mRNA 3'-end processing. Specific component of the tight junction (TJ) plaque, but might not be an exclusively junctional component. May have a house-keeping rule. Is involved in pre-mRNA polyadenylation. Enhances SSU72 phosphatase activity.<ref>PMID:16230528</ref> <ref>PMID:20861839</ref>  [[http://www.uniprot.org/uniprot/SSU72_HUMAN SSU72_HUMAN]] Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination. Plays a role in pre-mRNA polyadenylation via its interaction with SYMPK.<ref>PMID:15659578</ref> <ref>PMID:20861839</ref> <ref>PMID:23070812</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4h3k

From Proteopedia

Revision as of 22:55, 24 December 2014

Crystal structure of a ternary complex of human symplekin NTD, human Ssu72 and a RNA polymerase II CTD peptide phosphorylated at Ser-2, Ser-5 and Ser-7

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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