1EUW: ATOMIC RESOLUTION STRUCTURE OF E. COLI DUTPASE

Citation:
Abstract
Cryocooled crystals of a mercury complex of Escherichia coli dUTPase diffract to atomic resolution. Data to 1.05 A resolution were collected from a derivative crystal and the structure model was derived from a Fourier map with phases calculated from the coordinates of the Hg atom (one site per subunit of the trimeric enzyme) using the program ARP/wARP. After refinement with anisotropic temperature factors a highly accurate model of the bacterial dUTPase was obtained. Data to 1.45 A from a native crystal were also collected and the 100 K structures were compared. Inspection of the refined models reveals that a large part of the dUTPase remains rather mobile upon freezing, with 14% of the main chain being totally disordered and with numerous side chains containing disordered atoms in multiple discrete conformations. A large number of those residues surround the active-site cavity. Two glycerol molecules (the cryosolvent) occupy the deoxyribose-binding site. Comparison between the native enzyme and the mercury complex shows that the active site is not adversely affected by the binding of mercury. An unexpected effect seems to be a stabilization of the crystal lattice by means of long-range interactions, making derivatization a potentially useful tool for further studies of inhibitor-substrate-analogue complexes of this protein at very high resolution.
PDB ID: 1EUWDownload
MMDB ID: 163359
PDB Deposition Date: 2000/4/17
Updated in MMDB: 2018/06
Experimental Method:
x-ray diffraction
Resolution: 1.05  Å
Source Organism:
Similar Structures:
Biological Unit for 1EUW: trimeric; determined by author and by software (PISA,PQS)
Molecular Components in 1EUW
Label Count Molecule
Proteins (3 molecules)
3
Deoxyuridine 5'-triphosphate Nucleotidohydrolase(Gene symbol: dut)
Molecule annotation
Chemicals (9 molecules)
1
3
2
6
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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