4g56
From Proteopedia
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===Crystal Structure of full length PRMT5/MEP50 complexes from Xenopus laevis=== | ===Crystal Structure of full length PRMT5/MEP50 complexes from Xenopus laevis=== | ||
{{ABSTRACT_PUBMED_23451136}} | {{ABSTRACT_PUBMED_23451136}} | ||
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| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/ANM5_XENLA ANM5_XENLA]] Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins; such methylation being required for the assembly and biogenesis of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation (By similarity). Methylates the arginine in the motif G-R-G-X-G in its substrates histone H2A, H2AFX and H4, producing both monomethylated and symmetrically dimethylated 'Arg-3'. Methylates nucleoplasmin at 'Arg-192', producing both monomethylated and symmetrically dimethylated 'Arg-192'. Involved in the DNA replication checkpoint. Promotes entry into mitosis by promoting the proteasomal degradation of wee2-a. [[http://www.uniprot.org/uniprot/MEP50_XENLA MEP50_XENLA]] Non-catalytic component of the 20S prmt5-containing methyltransferase complex, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones. Required for normal prmt5 methyltransferase activity. | ||
==About this Structure== | ==About this Structure== | ||
[[4g56]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G56 OCA]. | [[4g56]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G56 OCA]. | ||
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| + | ==Reference== | ||
| + | <ref group="xtra">PMID:023451136</ref><references group="xtra"/><references/> | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
[[Category: Almo, S C.]] | [[Category: Almo, S C.]] | ||
[[Category: Bonanno, J.]] | [[Category: Bonanno, J.]] | ||
[[Category: Ho, M.]] | [[Category: Ho, M.]] | ||
| + | [[Category: NYSGRC, New York Structural Genomics Research Consortium.]] | ||
[[Category: Shechter, D.]] | [[Category: Shechter, D.]] | ||
[[Category: Wilczek, C.]] | [[Category: Wilczek, C.]] | ||
Revision as of 09:09, 4 September 2013
Contents |
Crystal Structure of full length PRMT5/MEP50 complexes from Xenopus laevis
Template:ABSTRACT PUBMED 23451136
Function
[ANM5_XENLA] Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins; such methylation being required for the assembly and biogenesis of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation (By similarity). Methylates the arginine in the motif G-R-G-X-G in its substrates histone H2A, H2AFX and H4, producing both monomethylated and symmetrically dimethylated 'Arg-3'. Methylates nucleoplasmin at 'Arg-192', producing both monomethylated and symmetrically dimethylated 'Arg-192'. Involved in the DNA replication checkpoint. Promotes entry into mitosis by promoting the proteasomal degradation of wee2-a. [MEP50_XENLA] Non-catalytic component of the 20S prmt5-containing methyltransferase complex, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones. Required for normal prmt5 methyltransferase activity.
About this Structure
4g56 is a 4 chain structure with sequence from Xenopus laevis. Full crystallographic information is available from OCA.
Reference
- Ho MC, Wilczek C, Bonanno JB, Xing L, Seznec J, Matsui T, Carter LG, Onikubo T, Kumar PR, Chan MK, Brenowitz M, Cheng RH, Reimer U, Almo SC, Shechter D. Structure of the Arginine Methyltransferase PRMT5-MEP50 Reveals a Mechanism for Substrate Specificity. PLoS One. 2013;8(2):e57008. doi: 10.1371/journal.pone.0057008. Epub 2013 Feb 25. PMID:23451136 doi:10.1371/journal.pone.0057008
