› 2pun

X-ray diffraction
2.3Å resolution

Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding

Released:
DOI: 10.2210/pdb2pun/pdb
PDB entry 2pun coloured by chain, front view.
PDB entry 2pun coloured by chain, side view.
PDB entry 2pun coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding.
Ku SY, Yip P, Cornell KA, Riscoe MK, Behr JB, Guillerm G, Howell PL
J Biol Chem 282 22195-206 (2007)
PMID: 17522047

Function and Biology Details

Reaction catalysed: 
ATP + S-methyl-5-thio-D-ribose = ADP + S-methyl-5-thio-alpha-D-ribose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-128324 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methylthioribose kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 397 amino acids
Theoretical weight: 45.14 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O31663 (Residues: 1-397; Coverage: 100%)
Gene names: BSU13560, mtnK, ykrT
Sequence domains: Phosphotransferase enzyme family
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand MG 2 x MG
Ligand CPS 1 x CPS
Ligand ACP 2 x ACP
Ligand SR1 2 x SR1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21212
Unit cell:
a: 214.73Å b: 83.62Å c: 51.17Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.202 0.255
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

The genomic enzymology of antibiotic resistance.
Morar et al. (2010)
1 more

4 mentions without citation

Structure of the antibiotic resistance factor spectinomycin phosphotransferase from Legionella pneumophila.
Fong et al. (2010)
3 more