1soi

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spinqualitylabelsall models 1soi, resolution 1.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF NUDIX HYDROLASE DR1025 IN COMPLEX WITH SM+3

Overview

We have determined the crystal structure, at 1.4A, 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 beta-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 Ap(4)A (both at 1.6A resolution). In, the Ap(4)A co-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.

About this Structure

1SOI is a Single protein structure of sequence from Deinococcus radiodurans with SM as ligand. Full crystallographic information is available from OCA.

Reference

Structural studies of the Nudix hydrolase DR1025 from Deinococcus radiodurans and its ligand complexes., Ranatunga W, Hill EE, Mooster JL, Holbrook EL, Schulze-Gahmen U, Xu W, Bessman MJ, Brenner SE, Holbrook SR, J Mol Biol. 2004 May 21;339(1):103-16. PMID:15123424

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