4G56

Crystal Structure of full length PRMT5/MEP50 complexes from Xenopus laevis

Summary for 4G56

• Entry DOI: 10.2210/pdb4g56/pdb
• Descriptor: Hsl7 protein, MGC81050 protein, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total)
• Functional Keywords: protein arginine methyltransferase, protein complexes, histone methylation, transferase, structural genomics, psi-biology, new york structural genomics research consortium, nysgrc
• Biological source: Xenopus laevis (clawed frog,common platanna,platanna); More
• Cellular location: Cytoplasm: Q6NUA1 Q6NUD0
• Total number of polymer chains: 4
• Total formula weight: 229941.22

Authors

Ho, M.,Wilczek, C.,Bonanno, J.,Shechter, D.,Almo, S.C.,New York Structural Genomics Research Consortium (NYSGRC) (deposition date: 2012-07-17, release date: 2012-10-03, Last modification date: 2017-11-15)

• Primary citation: Ho, M.C.,Wilczek, C.,Bonanno, J.B.,Xing, L.,Seznec, J.,Matsui, T.,Carter, L.G.,Onikubo, T.,Kumar, P.R.,Chan, M.K.,Brenowitz, M.,Cheng, R.H.,Reimer, U.,Almo, S.C.,Shechter, D.; Structure of the arginine methyltransferase PRMT5-MEP50 reveals a mechanism for substrate specificity; Plos One, 8:e57008-e57008, 2013; PubMed: 23451136; DOI: 10.1371/journal.pone.0057008

Experimental method

X-RAY DIFFRACTION (2.95 Å)