5DST

Crystal structure of human PRMT8 in complex with SAH


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.96 Å
  • R-Value Free: 0.260 
  • R-Value Work: 0.224 
  • R-Value Observed: 0.225 

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Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Novel helical assembly in arginine methyltransferase 8

Toma-Fukai, S.Kim, J.D.Park, K.E.Kuwabara, N.Shimizu, N.Krayukhina, E.Uchiyama, S.Fukamizu, A.Shimizu, T.

(2016) J Mol Biol 428: 1197-1208

  • DOI: https://doi.org/10.1016/j.jmb.2016.02.007
  • Primary Citation of Related Structures:  
    5DST

  • PubMed Abstract: 

    Protein arginine methyltransferase 8 (PRMT8) is unique among PRMTs, as it is specifically expressed in brain and localized to the plasma membrane via N-terminal myristoylation. Here, we describe the crystal structure of human PRMT8 (hPRMT8) at 3.0-Å resolution. The crystal structure of hPRMT8 exhibited a novel helical assembly. Biochemical, biophysical and mutagenesis experiments demonstrated that hPRMT8 forms an octamer in solution. This octameric structure is necessary for proper localization to the plasma membrane and efficient methyltransferase activity. The helical assembly might be a relevant quaternary form for hPRMT1, which is the predominant PRMT in mammalian cells and most closely related to hPRMT8.


  • Organizational Affiliation

    Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Protein arginine N-methyltransferase 8
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O
332Homo sapiensMutation(s): 0 
Gene Names: PRMT8HRMT1L3HRMT1L4
EC: 2.1.1
UniProt & NIH Common Fund Data Resources
Find proteins for Q9NR22 (Homo sapiens)
Explore Q9NR22 
Go to UniProtKB:  Q9NR22
PHAROS:  Q9NR22
GTEx:  ENSG00000111218 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9NR22
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
SAH
Query on SAH

Download Ideal Coordinates CCD File 
AA [auth L]
BA [auth M]
CA [auth N]
DA [auth O]
P [auth A]
AA [auth L],
BA [auth M],
CA [auth N],
DA [auth O],
P [auth A],
Q [auth B],
R [auth C],
S [auth D],
T [auth E],
U [auth F],
V [auth G],
W [auth H],
X [auth I],
Y [auth J],
Z [auth K]
S-ADENOSYL-L-HOMOCYSTEINE
C14 H20 N6 O5 S
ZJUKTBDSGOFHSH-WFMPWKQPSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.96 Å
  • R-Value Free: 0.260 
  • R-Value Work: 0.224 
  • R-Value Observed: 0.225 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 199.983α = 90
b = 130.943β = 106.48
c = 294.377γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data reduction
SCALEPACKdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Japan--

Revision History  (Full details and data files)

  • Version 1.0: 2016-02-24
    Type: Initial release
  • Version 1.1: 2016-04-20
    Changes: Database references
  • Version 1.2: 2020-02-19
    Changes: Data collection, Database references, Derived calculations
  • Version 1.3: 2024-03-20
    Changes: Data collection, Database references, Refinement description