2P5X

Crystal structure of Maf domain of human N-acetylserotonin O-methyltransferase-like protein


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.253 
  • R-Value Work: 0.198 
  • R-Value Observed: 0.201 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Biochemical and structural studies of conserved maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides.

Tchigvintsev, A.Tchigvintsev, D.Flick, R.Popovic, A.Dong, A.Xu, X.Brown, G.Lu, W.Wu, H.Cui, H.Dombrowski, L.Joo, J.C.Beloglazova, N.Min, J.Savchenko, A.Caudy, A.A.Rabinowitz, J.D.Murzin, A.G.Yakunin, A.F.

(2013) Chem Biol 20: 1386-1398

  • DOI: https://doi.org/10.1016/j.chembiol.2013.09.011
  • Primary Citation of Related Structures:  
    2P5X, 4HEB, 4JHC, 4LU1

  • PubMed Abstract: 

    Maf (for multicopy associated filamentation) proteins represent a large family of conserved proteins implicated in cell division arrest but whose biochemical activity remains unknown. Here, we show that the prokaryotic and eukaryotic Maf proteins exhibit nucleotide pyrophosphatase activity against 5-methyl-UTP, pseudo-UTP, 5-methyl-CTP, and 7-methyl-GTP, which represent the most abundant modified bases in all organisms, as well as against canonical nucleotides dTTP, UTP, and CTP. Overexpression of the Maf protein YhdE in E. coli cells increased intracellular levels of dTMP and UMP, confirming that dTTP and UTP are the in vivo substrates of this protein. Crystal structures and site-directed mutagenesis of Maf proteins revealed the determinants of their activity and substrate specificity. Thus, pyrophosphatase activity of Maf proteins toward canonical and modified nucleotides might provide the molecular mechanism for a dual role of these proteins in cell division arrest and house cleaning.


  • Organizational Affiliation

    Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, ON M5S 3E5, Canada.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
N-acetylserotonin O-methyltransferase-like protein
A, B
230Homo sapiensMutation(s): 0 
Gene Names: ASMTL
UniProt & NIH Common Fund Data Resources
Find proteins for O95671 (Homo sapiens)
Explore O95671 
Go to UniProtKB:  O95671
PHAROS:  O95671
GTEx:  ENSG00000169093 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO95671
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.253 
  • R-Value Work: 0.198 
  • R-Value Observed: 0.201 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 84.802α = 90
b = 116.983β = 90
c = 51.471γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
CrystalCleardata collection
HKL-2000data reduction
HKL-2000data scaling
MOLREPphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2007-03-27
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.3: 2013-11-20
    Changes: Database references, Structure summary
  • Version 1.4: 2014-01-15
    Changes: Database references
  • Version 1.5: 2023-08-30
    Changes: Data collection, Database references, Derived calculations, Refinement description