1SZ3

CRYSTAL STRUCTURE OF NUDIX HYDROLASE DR1025 IN COMPLEXED WITH GNP AND MG+2

1SZ3 の概要

• エントリーDOI: 10.2210/pdb1sz3/pdb
• 分子名称: MutT/nudix family protein, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (4 entities in total)
• 機能のキーワード: nudix fold, alpha-beta-alpha sandwich, structural genomics, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center, hydrolase
• 由来する生物種: Deinococcus radiodurans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36272.87

構造登録者

Ranatunga, W.,Hill, E.E.,Mooster, J.L.,Holbrook, E.L.,Schulze-Gahmen, U.,Xu, W.,Bessman, M.J.,Brenner, S.E.,Holbrook, S.R.,Berkeley Structural Genomics Center (BSGC) (登録日: 2004-04-02, 公開日: 2004-05-11, 最終更新日: 2024-02-14)

主引用文献

Ranatunga, W.,Hill, E.E.,Mooster, J.L.,Holbrook, E.L.,Schulze-Gahmen, U.,Xu, W.,Bessman, M.J.,Brenner, S.E.,Holbrook, S.R.
Structural Studies of the Nudix Hydrolase DR1025 From Deinococcus radiodurans and its Ligand Complexes.
J.Mol.Biol., 339:103-116, 2004

PubMed Abstract: 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.

PubMed: 15123424
DOI: 10.1016/j.jmb.2004.01.065

実験手法

X-RAY DIFFRACTION (1.6 Å)