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PDBsum entry 4g56
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protein ligands Protein-protein interface(s) links
Transferase PDB id
4g56

 

 

 

 

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Contents
Protein chains
617 a.a.
292 a.a.
Ligands
SAH ×2
Waters ×9
PDB id:
4g56
Name: Transferase
Title: Crystal structure of full length prmt5/mep50 complexes from xenopus laevis
Structure: Hsl7 protein. Chain: a, c. Fragment: unp residues 2-633. Synonym: methyltransferase hsl7. Engineered: yes. Mgc81050 protein. Chain: b, d. Fragment: unp residues 2-333. Engineered: yes
Source: Xenopus laevis. Clawed frog,common platanna,platanna. Organism_taxid: 8355. Gene: hsl7, prmt5. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Gene: mep50, mgc81050, wdr77.
Resolution:
2.95Å     R-factor:   0.220     R-free:   0.276
Authors: M.Ho,C.Wilczek,J.Bonanno,D.Shechter,S.C.Almo,New York Structural Genomics Research Consortium (Nysgrc)
Key ref: M.C.Ho et al. (2013). Structure of the arginine methyltransferase PRMT5-MEP50 reveals a mechanism for substrate specificity. Plos One, 8, e57008. PubMed id: 23451136 DOI: 10.1371/journal.pone.0057008
Date:
17-Jul-12     Release date:   03-Oct-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q6NUA1  (ANM5_XENLA) -  Protein arginine N-methyltransferase 5 from Xenopus laevis
Seq:
Struc: 		 
Seq:
Struc: 		633 a.a.
617 a.a.
Protein chains
Pfam   ArchSchema ?
Q6NUD0  (MEP50_XENLA) -  Methylosome protein WDR77 from Xenopus laevis
Seq:
Struc: 		333 a.a.
292 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, C: E.C.2.1.1.320  - type Ii protein arginine methyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L- homocysteine + 2 H+
L-arginyl-[protein]
Bound ligand (Het Group name = SAH)
matches with 96.30% similarity 		+ 2 × S-adenosyl-L-methionine
 = N(omega),N(omega)'-dimethyl-L-arginyl-[protein]
 + 2 × S-adenosyl-L- homocysteine
 + 2 × H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1371/journal.pone.0057008 Plos One 8:e57008 (2013)
PubMed id: 23451136  
 
 
Structure of the arginine methyltransferase PRMT5-MEP50 reveals a mechanism for substrate specificity.
M.C.Ho, C.Wilczek, J.B.Bonanno, L.Xing, J.Seznec, T.Matsui, L.G.Carter, T.Onikubo, P.R.Kumar, M.K.Chan, M.Brenowitz, R.H.Cheng, U.Reimer, S.C.Almo, D.Shechter.
 
  ABSTRACT  
 
No abstract given.

 

 

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