› 4ojt

X-ray diffraction
1.5Å resolution

Helicobacter pylori MTAN complexed with S-ribosylhomocysteine and adenine

Released:
DOI: 10.2210/pdb4ojt/pdb
PDB entry 4ojt coloured by chain, front view.
PDB entry 4ojt coloured by chain, side view.
PDB entry 4ojt coloured by chain, top view.
Source organism: Helicobacter pylori J99
Primary publication:
Crystal structures of the Helicobacter pylori MTAN enzyme reveal specific interactions between S-adenosylhomocysteine and the 5'-alkylthio binding subsite.
Mishra V, Ronning DR
Biochemistry 51 9763-72 (2012)
PMID: 23148563

Function and Biology Details

Reactions catalysed: 
6-amino-6-deoxyfutalosine + H(2)O = dehypoxanthine futalosine + adenine
5'-deoxyadenosine + H(2)O = 5-deoxy-D-ribose + adenine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-579264 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminodeoxyfutalosine nucleosidase Chain: A
Molecule details ›
Chain: A
Length: 231 amino acids
Theoretical weight: 25.11 KDa
Source organism: Helicobacter pylori J99
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9ZMY2 (Residues: 2-230; Coverage: 100%)
Gene names: jhp_0082, mtn, mtnN
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

2 bound ligands:
Ligand 2WP 1 x 2WP
Ligand ADE 1 x ADE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P3221
Unit cell:
a: 81.241Å b: 81.241Å c: 67.456Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.182 0.205
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Molecular architectures and functions of radical enzymes and their (re)activating proteins.
Shibata et al. (2015)
10 other articles

1 mention without citation

Characterization of Ionizable Groups' Environments in Proteins and Protein-Ligand Complexes through a Statistical Analysis of the Protein Data Bank.
Borrel et al. (2017)