 |
PDBsum entry 1dup
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure of a dutpase.
|
|
|
Authors
|
|
E.S.Cedergren-Zeppezauer,
G.Larsson,
P.O.Nyman,
Z.Dauter,
K.S.Wilson.
|
|
|
Ref.
|
|
Nature, 1992,
355,
740-743.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The enzyme dUTPase catalyses the hydrolysis of dUTP and maintains a low
intracellular concentration of dUTP so that uracil cannot be incorporated into
DNA. dUTPase from Escherichia coli is strictly specific for its dUTP substrate,
the active site discriminating between nucleotides with respect to the sugar
moiety as well as the pyrimidine base. Here we report the three-dimensional
structure of E. coli dUTPase determined by X-ray crystallography at a resolution
of 1.9 A. The enzyme is a symmetrical trimer, and of the 152 amino acid residues
in the subunit, the first 136 are visible in the crystal structure. The tertiary
structure resembles a jelly-roll fold and does not show the 'classical'
nucleotide-binding domain. In the quaternary structure there is a complex
interaction between the subunits that may be important in catalysis. This
possibility is supported by the location of conserved elements in the sequence.
|
|
|
|
|
|
|
