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PDBsum entry 4gqb
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Transferase/protein binding
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PDB id
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4gqb
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PDB id:
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| Name: |
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Transferase/protein binding
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Title:
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Crystal structure of the human prmt5:mep50 complex
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Structure:
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Protein arginine n-methyltransferase 5. Chain: a. Synonym: 72 kda icln-binding protein, histone-arginine n- methyltransferase prmt5, jak-binding protein 1, shk1 kinase-binding protein 1 homolog, skb1 homolog, skb1hs, protein arginine n- methyltransferase 5, n-terminally processed. Engineered: yes. Methylosome protein 50. Chain: b.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: prmt5, hrmt1l5, ibp72, jbp1, skb1. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Gene: wdr77, mep50, hkmt1069, nbla10071. Synthetic: yes. Organism_taxid: 9606
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Resolution:
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2.06Å
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R-factor:
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0.190
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R-free:
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0.222
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Authors:
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S.Antonysamy,Z.Bonday,R.Campbell,B.Doyle,Z.Druzina,T.Gheyi,B.Han, L.N.Jungheim,Y.Qian,C.Rauch,M.Russell,J.M.Sauder,S.R.Wasserman, K.Weichert,F.S.Willard,A.Zhang,S.Emtage
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Key ref:
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S.Antonysamy
et al.
(2012).
Crystal structure of the human PRMT5:MEP50 complex.
Proc Natl Acad Sci U S A,
109,
17960-17965.
PubMed id:
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Date:
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22-Aug-12
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Release date:
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17-Oct-12
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PROCHECK
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Headers
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References
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Enzyme class:
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Chain A:
E.C.2.1.1.320
- type Ii protein arginine methyltransferase.
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Reaction:
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L-arginyl-[protein] + 2 S-adenosyl-L-methionine = N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L- homocysteine + 2 H+
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L-arginyl-[protein]
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+
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2
×
S-adenosyl-L-methionine
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=
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N(omega),N(omega)'-dimethyl-L-arginyl-[protein]
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+
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2
×
S-adenosyl-L- homocysteine
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+
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2
×
H(+)
Bound ligand (Het Group name = )
matches with 51.43% similarity
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Proc Natl Acad Sci U S A
109:17960-17965
(2012)
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PubMed id:
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Crystal structure of the human PRMT5:MEP50 complex.
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S.Antonysamy,
Z.Bonday,
R.M.Campbell,
B.Doyle,
Z.Druzina,
T.Gheyi,
B.Han,
L.N.Jungheim,
Y.Qian,
C.Rauch,
M.Russell,
J.M.Sauder,
S.R.Wasserman,
K.Weichert,
F.S.Willard,
A.Zhang,
S.Emtage.
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ABSTRACT
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Protein arginine methyltransferases (PRMTs) play important roles in several
cellular processes, including signaling, gene regulation, and transport of
proteins and nucleic acids, to impact growth, differentiation, proliferation,
and development. PRMT5 symmetrically di-methylates the two-terminal ω-guanidino
nitrogens of arginine residues on substrate proteins. PRMT5 acts as part of a
multimeric complex in concert with a variety of partner proteins that regulate
its function and specificity. A core component of these complexes is the WD40
protein MEP50/WDR77/p44, which mediates interactions with binding partners and
substrates. We have determined the crystal structure of human PRMT5 in complex
with MEP50 (methylosome protein 50), bound to an S-adenosylmethionine analog and
a peptide substrate derived from histone H4. The structure of the surprising
hetero-octameric complex reveals the close interaction between the seven-bladed
β-propeller MEP50 and the N-terminal domain of PRMT5, and delineates the
structural elements of substrate recognition.
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Links
