1Q27

NMR Solution Structure of DR0079: An hypothetical Nudix protein from D. radiodurans

Summary for 1Q27

• Entry DOI: 10.2210/pdb1q27/pdb
• NMR Information: BMRB: 5570
• Descriptor: Putative Nudix hydrolase DR0079 (1 entity in total)
• Functional Keywords: nudix hydrolase, radiation resistance, hydrolase
• Biological source: Deinococcus radiodurans
• Total number of polymer chains: 1
• Total formula weight: 19303.56

Authors

Buchko, G.W.,Ni, S.,Holbrook, S.R.,Kennedy, M.A. (deposition date: 2003-07-23, release date: 2003-08-12, Last modification date: 2024-05-22)

Primary citation

Buchko, G.W.,Ni, S.,Holbrook, S.R.,Kennedy, M.A.
Solution structure of hypothetical Nudix hydrolase DR0079 from extremely radiation-resistant Deinococcus radiodurans bacterium
Proteins, 56:28-39, 2004

PubMed Abstract: Using nuclear magnetic resonance (NMR) based methods, including residual dipolar coupling restraints, we have determined the solution structure of the hypothetical Deinococcus radiodurans Nudix protein DR0079 (171 residues, MW = 19.3 kDa). The protein contains eight beta-strands and three alpha-helices organized into three subdomains: an N-terminal beta-sheet (1-34), a central Nudix core (35-140), and a C-terminal helix-turn-helix (141-171). The Nudix core and the C-terminal helix-turn-helix form the fundamental fold common to the Nudix family, a large mixed beta-sheet sandwiched between alpha-helices. The residues that compose the signature Nudix sequence, GX5EX7REUXEEXGU (where U = I, L, or V and X = any amino acid), are contained in a turn-helix-turn motif on the face of the mixed beta-sheet. Chemical shift mapping experiments suggest that DR0079 binds Mg2+. Experiments designed to determine the biological function of the protein indicate that it is not a type I isopentenyl-diphosphate delta-isomerase and that it does not bind alpha,beta-methyleneadenosine 5'-triphosphate (AMPCPP) or guanosine 5'-[beta,gamma-imido]triphosphate (GMPPNP). In this article, the structure of DR0079 is compared to other known Nudix protein structures, a potential substrate-binding surface is proposed, and its possible biological function is discussed.

PubMed: 15162484
DOI: 10.1002/prot.20082

Experimental method

SOLUTION NMR