PDBsum entry 2b7n

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Transferase PDB id
Protein chains
273 a.a. *
SO4 ×3
NTM ×3
Waters ×210
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Crystal structure of quinolinic acid phosphoribosyltransfera helicobacter pylori
Structure: Probable nicotinate-nucleotide pyrophosphorylase. Chain: a, b, c. Synonym: quinolinate phosphoribosyltransferase, decarboxyla qaprtase. Engineered: yes
Source: Helicobacter pylori. Organism_taxid: 210. Expressed in: escherichia coli. Expression_system_taxid: 562
2.30Å     R-factor:   0.224     R-free:   0.256
Authors: M.K.Kim,Y.J.Im,J.H.Lee,S.H.Eom
Key ref:
M.K.Kim et al. (2006). Crystal structure of quinolinic acid phosphoribosyltransferase from Helicobacter pylori. Proteins, 63, 252-255. PubMed id: 16419067 DOI: 10.1002/prot.20834
04-Oct-05     Release date:   14-Feb-06    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
O25909  (NADC_HELPY) -  Probable nicotinate-nucleotide pyrophosphorylase [carboxylating]
273 a.a.
273 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Nicotinate-nucleotide diphosphorylase (carboxylating).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Beta-nicotinate D-ribonucleotide + diphosphate + CO2 = pyridine-2,3- dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate
Beta-nicotinate D-ribonucleotide
+ diphosphate
+ CO(2)
pyridine-2,3- dicarboxylate
Bound ligand (Het Group name = NTM)
corresponds exactly
+ 5-phospho-alpha-D-ribose 1-diphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     pyridine nucleotide biosynthetic process   2 terms 
  Biochemical function     catalytic activity     5 terms  


DOI no: 10.1002/prot.20834 Proteins 63:252-255 (2006)
PubMed id: 16419067  
Crystal structure of quinolinic acid phosphoribosyltransferase from Helicobacter pylori.
M.K.Kim, Y.J.Im, J.H.Lee, S.H.Eom.
No abstract given.

  Selected figure(s)  
Figure 1.
Figure 1. Crystal structure of Hp-QAPRTase. (A) Ribbon diagram of the Hp-QAPRTase monomer. The N-terminal domain (residues 1-116, 258-273) is shown in yellow, and the C-terminal domain (residue 117-257) in orange. QA is shown as a space filling model. (B) Structure of the Hp-QAPRTase dimer. (C) QA binding site. The side chains at the active site are shown as a ball-and-stick model. (D) NAMN-binding site. The 2Fo-Fc electron density map contoured at 1s. (E) Structure of the Hp-QAPRTase hexamer. (F). Surface representation of the Hp-QAPRTase hexamer. The side chains of Phe181 at the interface of the subunits are shown as a space filling model. All figures were prepared using the program PyMOL (
  The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2006, 63, 252-255) copyright 2006.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20047306 Z.Bello, and C.Grubmeyer (2010).
Roles for cationic residues at the quinolinic acid binding site of quinolinate phosphoribosyltransferase.
  Biochemistry, 49, 1388-1395.  
17763926 M.K.Kim, G.B.Kang, W.K.Song, and S.H.Eom (2007).
The role of Phe181 in the hexamerization of Helicobacter pylori quinolinate phosphoribosyltransferase.
  Protein J, 26, 517-521.  
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