Structural studies of the nudix hydrolase DR1025 from deinococcus radiodurans and its ligand complexes
We have determined the crystal structure, at 1.4, of the Nudix hydrolase DR1025 from the extremely radiation resistant bacterium Deinococcus radiodurans. The protein forms an intertwined homodimer by exchanging N-terminal segments between chains. We have identified additional conserved elements of the Nudix fold, including the metal-binding motif, a kinked b-strand characterized by a proline two positions upstream of the Nudix consensus sequence, and participation of the N-terminal extension in the formation of the substrate-binding pocket. Crystal structures were also solved of DR1025 crystallized in the presence of magnesium and either a GTP analog or Ap4A (both at 1.6 resolution). In the Ap4Aco-crystal, the electron density indicated that the product of asymmetric hydrolysis, ATP, was bound to the enzyme. The GTP analog bound structure showed that GTP was bound almost identically as ATP. Neither nucleoside triphosphate was further cleaved.
- Research Organization:
- Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
- Sponsoring Organization:
- USDOE Director. Office of Science. Office of Biological and Environmental Research; National Institutes of Health Grants 1-K22-HG00056 and GM 18649 (US)
- DOE Contract Number:
- AC03-76SF00098
- OSTI ID:
- 840389
- Report Number(s):
- LBNL-55044; JMOBAK; R&D Project: 4488SH; TRN: US200510%%135
- Journal Information:
- Journal of Molecular Biology, Vol. 339; Other Information: Journal Publication Date: 2004; PBD: 29 Jan 2004; ISSN 0022-2836
- Country of Publication:
- United States
- Language:
- English
Similar Records
Functional and Structural Characterization of DR_0079 from Deinococcus radiodurans, a Novel Nudix Hydrolase with a Preference for Cytosine (Deoxy)ribonucleoside 5 -Di- and Triphophates
H-1, C-13, and N-15 NMR assignments of the hypothetical Nudix protein DR0079 from the extremely radiation-resistant bacterium Deinococcus radiodurans.