1q27 | pdb_00001q27
NMR Solution Structure of DR0079: An hypothetical Nudix protein from D. radiodurans
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Overview
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.
About this Structure
1Q27 is a Single protein structure of sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA.
Reference
Solution structure of hypothetical Nudix hydrolase DR0079 from extremely radiation-resistant Deinococcus radiodurans bacterium., Buchko GW, Ni S, Holbrook SR, Kennedy MA, Proteins. 2004 Jul 1;56(1):28-39. PMID:15162484
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