Literature summary for 2.1.1.320 extracted from

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 (2013), PLoS ONE, 8, e57008.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
complex of isoform PRMT5, methylosome protein MEP50 and S-adenosylhomocysteine. PRMT5-MEP50 forms an unusual tetramer of heterodimers with substantial surface negative charge. MEP50 is required for PRMT5-catalyzed histone H2A and H4 methyltransferase activity and binds substrates independently. MEP50 binds to the substrate distal of the target arginine and orients the unstructured substrate tail towards the catalytic site of the PRMT5 molecule that is not directly coupled to the substrate-bound MEP50	Xenopus laevis

Crystallization (Comment)

Organism

complex of isoform PRMT5, methylosome protein MEP50 and S-adenosylhomocysteine. PRMT5-MEP50 forms an unusual tetramer of heterodimers with substantial surface negative charge. MEP50 is required for PRMT5-catalyzed histone H2A and H4 methyltransferase activity and binds substrates independently. MEP50 binds to the substrate distal of the target arginine and orients the unstructured substrate tail towards the catalytic site of the PRMT5 molecule that is not directly coupled to the substrate-bound MEP50

Xenopus laevis

Organism

Organism	UniProt	Comment	Textmining
Xenopus laevis	Q6NUA1	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	PRMT5-MEP50 activity is inhibited by substrate phosphorylation and enhanced by substrate acetylation	Xenopus laevis	?	-	?

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Release 2023.1 (January 2023)