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PDBsum entry 1og4

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protein ligands links
Transferase PDB id
1og4
Jmol
Contents
Protein chain
223 a.a. *
Ligands
NAI
Waters ×138
* Residue conservation analysis
PDB id:
1og4
Name: Transferase
Title: Crystal structure of the eucaryotic mono-adp-ribosyltransferase art2.2 mutant e189a in complex with nadh
Structure: T-cell ecto-adp-ribosyltransferase 2. Chain: a. Fragment: residues 21-246. Engineered: yes. Mutation: yes
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.6Å     R-factor:   0.196     R-free:   0.254
Authors: H.Ritter,F.Koch-Nolte,V.E.Marquez,G.E.Schulz
Key ref:
H.Ritter et al. (2003). Substrate binding and catalysis of ecto-ADP-ribosyltransferase 2.2 from rat. Biochemistry, 42, 10155-10162. PubMed id: 12939142 DOI: 10.1021/bi034625w
Date:
24-Apr-03     Release date:   28-Aug-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P20974  (NAR2B_RAT) -  T-cell ecto-ADP-ribosyltransferase 2
Seq:
Struc:
275 a.a.
223 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.4.2.31  - NAD(+)--protein-arginine ADP-ribosyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: NAD+ + protein-L-arginine = nicotinamide + N(omega)-(ADP-D-ribosyl)- protein-L-arginine
NAD(+)
Bound ligand (Het Group name = NAI)
corresponds exactly
+ protein-L-arginine
= nicotinamide
+ N(omega)-(ADP-D-ribosyl)- protein-L-arginine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     protein ADP-ribosylation   1 term 
  Biochemical function     NAD(P)+-protein-arginine ADP-ribosyltransferase activity     1 term  

 

 
    reference    
 
 
DOI no: 10.1021/bi034625w Biochemistry 42:10155-10162 (2003)
PubMed id: 12939142  
 
 
Substrate binding and catalysis of ecto-ADP-ribosyltransferase 2.2 from rat.
H.Ritter, F.Koch-Nolte, V.E.Marquez, G.E.Schulz.
 
  ABSTRACT  
 
The structures of beta-methylenethiazole-4-carboxamide adenine dinucleotide (TAD), NAD(+), and NADH as bound to ecto-ADP-ribosyltransferase 2.2 from rat and to its mutants E189I and E189A, respectively, have been established. The positions and conformations of NAD(+) and its analogues agree in general with those in other ADP-ribosyltransferases. The kinetic constants for NAD(+) hydrolysis were determined by RP-HPLC. The specific activity amounts to 26 units/mg, which is 6000-fold higher than a previously reported rate and 500-fold higher than the hydrolysis rates of other ADP-ribosyltransferases, confirming that hydrolysis is the major function of this enzyme. On the basis of structures and mutant activities, a catalytic mechanism is proposed. The known auto-ADP-ribosylation of the enzyme at the suggested position R184 is supported by one of the crystal structures where the nucleophile position is occupied by an Neta atom of this arginine which in turn is backed up by the base E159.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21170356 R.J.Fieldhouse, Z.Turgeon, D.White, and A.R.Merrill (2010).
Cholera- and anthrax-like toxins are among several new ADP-ribosyltransferases.
  PLoS Comput Biol, 6, e1001029.  
19651868 C.Johnson, T.R.Kannan, and J.B.Baseman (2009).
Characterization of a unique ADP-ribosyltransferase of Mycoplasma penetrans.
  Infect Immun, 77, 4362-4370.  
18292897 I.Richter, J.Minari, P.Axe, J.P.Lowe, T.D.James, K.Sakurai, S.D.Bull, and J.S.Fossey (2008).
Intramolecular cation-pi interactions control the conformation of nonrestricted (phenylalkyl)pyridines.
  Chem Commun (Camb), (), 1082-1084.  
16892389 D.Bellocchi, G.Costantino, R.Pellicciari, N.Re, A.Marrone, and C.Coletti (2006).
Poly(ADP-ribose)-polymerase-catalyzed hydrolysis of NAD+: QM/MM simulation of the enzyme reaction.
  ChemMedChem, 1, 533-539.  
16956368 K.P.Holbourn, C.C.Shone, and K.R.Acharya (2006).
A family of killer toxins. Exploring the mechanism of ADP-ribosylating toxins.
  FEBS J, 273, 4579-4593.  
16202152 H.Otto, P.A.Reche, F.Bazan, K.Dittmar, F.Haag, and F.Koch-Nolte (2005).
In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs).
  BMC Genomics, 6, 139.  
16195877 S.Rothenburg, F.Haag, F.Koch-Nolte, C.Carter, M.Graham, and G.W.Butcher (2005).
Characterization of multiple alleles of the T-cell differentiation marker ART2 (RT6) in inbred and wild rats.
  Immunogenetics, 57, 739-749.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.