- Abstract:
-
dUTPases are housekeeping enzymes which catalyse the hydrolysis of dUTP to dUMP in an ion-dependent manner. Bacillus subtilis has both a genomic and an SPβ prophage homotrimeric dUTPase. Here, structure determination of the prophage apoenzyme and of its complexes with dUDP and dUpNHpp-Mg(2+) is described at 1.75, 1.9 and 2.55 Å resolution, respectively. The C-terminal extension, which carries the conserved motif V, is disordered in all three structures. Unlike all other trimeric dUTPases for ...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1107/s0907444911003234
-
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- Journal:
- Acta crystallographica. Section D, Biological crystallography
- Volume:
- 67
- Issue:
- Pt 3
- Pages:
- 167-175
- Publication date:
- 2011-03-05
- DOI:
- EISSN:
-
1399-0047
- ISSN:
-
0907-4449
- URN:
-
uuid:1e2469c7-a7df-4928-9c3f-59fa6d398f75
- Source identifiers:
-
120196
- Local pid:
- pubs:120196
- Language:
- English
- Keywords:
- Copyright date:
- 2011
Journal article
The structure of Bacillus subtilis SPβ prophage dUTPase and its complexes with two nucleotides.
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