PDBsum entry 2b7n

Transferase

PDB id: 2b7n

Contents

Protein chains

273 a.a. *

Ligands

SO4 ×3

NTM ×3

Waters ×210

* Residue conservation analysis

PDB id:

2b7n

Name:

Transferase

Title:

Crystal structure of quinolinic acid phosphoribosyltransferase from helicobacter pylori

Structure:

Probable nicotinate-nucleotide pyrophosphorylase. Chain: a, b, c. Synonym: quinolinate phosphoribosyltransferase, decarboxylating, qaprtase. Engineered: yes

Source:

Helicobacter pylori. Organism_taxid: 210. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

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

Date:

04-Oct-05 Release date: 14-Feb-06

Protein chains

O25909  (NADC_HELPY) -  Probable nicotinate-nucleotide pyrophosphorylase [carboxylating] from Helicobacter pylori (strain ATCC 700392 / 26695)

Seq: 273 a.a.

Struc: 273 a.a.

Enzyme reactions

• Enzyme class: E.C.2.4.2.19 - nicotinate-nucleotide diphosphorylase (carboxylating).
• Reaction: nicotinate beta-D-ribonucleotide + CO2 + diphosphate = quinolinate + 5-phospho-alpha-D-ribose 1-diphosphate + 2 H⁺

nicotinate beta-D-ribonucleotide + CO2 + diphosphate = quinolinate + 5-phospho-alpha-D-ribose 1-diphosphate + 2 × H(+) (Bound ligand (Het Group name = NTM) corresponds exactly)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

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.

ABSTRACT

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 (www.pymol.org).

The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2006, 63, 252-255) copyright 2006.