› 1saz

X-ray diffraction
2.5Å resolution

Membership in the ASKHA Superfamily: Enzymological Properties and Crystal Structure of Butyrate Kinase 2 from Thermotoga maritima

Released:
DOI: 10.2210/pdb1saz/pdb
PDB entry 1saz coloured by chain, front view.
PDB entry 1saz coloured by chain, side view.
PDB entry 1saz coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Crystal structure of butyrate kinase 2 from Thermotoga maritima, a member of the ASKHA superfamily of phosphotransferases.
Diao J, Hasson MS
J Bacteriol 191 2521-9 (2009)
PMID: 19201797

Function and Biology Details

Reaction catalysed: 
ATP + butanoate = ADP + butanoyl phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194878 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable butyrate kinase 2 Chain: A
Molecule details ›
Chain: A
Length: 381 amino acids
Theoretical weight: 43.47 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X278 (Residues: 1-375; Coverage: 100%)
Gene names: TM_1756, buk2
Sequence domains: Acetokinase family
Structure domains: Nucleotidyltransferase; domain 5

Ligands and Environments

3 bound ligands:
Ligand NA 1 x NA
Ligand ACP 1 x ACP
Ligand FMT 4 x FMT
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: I422
Unit cell:
a: 197.685Å b: 197.685Å c: 58.238Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.267
Expression system: Escherichia coli

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Citations

4 citation in other articles

Influence of fatty acid precursors, including food preservatives, on the growth and fatty acid composition of Listeria monocytogenes at 37 and 10degreesC.
Julotok et al. (2010)
3 more

3 mentions without citation

Structural and mechanistic investigations on Salmonella typhimurium acetate kinase (AckA): identification of a putative ligand binding pocket at the dimeric interface.
Chittori et al. (2012)
2 more