2QJO

crystal structure of a bifunctional NMN adenylyltransferase/ADP ribose pyrophosphatase (NadM) complexed with ADPRP and NAD from Synechocystis sp.

2QJO の概要

• エントリーDOI: 10.2210/pdb2qjo/pdb
• 分子名称: Bifunctional NMN adenylyltransferase/Nudix hydrolase, SULFATE ION, ADENOSINE-5-DIPHOSPHORIBOSE, ... (6 entities in total)
• 機能のキーワード: two individual domains, transferase, hydrolase
• 由来する生物種: Synechocystis sp.
• 細胞内の位置: Cytoplasm : Q55928
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 120951.21

構造登録者

Huang, N.,Sorci, L.,Zhang, X.,Brautigan, C.,Raffaelli, N.,Magni, G.,Grishin, N.V.,Osterman, A.,Zhang, H. (登録日: 2007-07-08, 公開日: 2008-03-11, 最終更新日: 2024-02-21)

主引用文献

Huang, N.,Sorci, L.,Zhang, X.,Brautigam, C.A.,Li, X.,Raffaelli, N.,Magni, G.,Grishin, N.V.,Osterman, A.L.,Zhang, H.
Bifunctional NMN Adenylyltransferase/ADP-Ribose Pyrophosphatase: Structure and Function in Bacterial NAD Metabolism.
Structure, 16:196-209, 2008

PubMed Abstract: Bacterial NadM-Nudix is a bifunctional enzyme containing a nicotinamide mononucleotide (NMN) adenylyltransferase and an ADP-ribose (ADPR) pyrophosphatase domain. While most members of this enzyme family, such as that from a model cyanobacterium Synechocystis sp., are involved primarily in nicotinamide adenine dinucleotide (NAD) salvage/recycling pathways, its close homolog in a category-A biodefense pathogen, Francisella tularensis, likely plays a central role in a recently discovered novel pathway of NAD de novo synthesis. The crystal structures of NadM-Nudix from both species, including their complexes with various ligands and catalytic metal ions, revealed detailed configurations of the substrate binding and catalytic sites in both domains. The structure of the N-terminal NadM domain may be exploited for designing new antitularemia therapeutics. The ADPR binding site in the C-terminal Nudix domain is substantially different from that of Escherichia coli ADPR pyrophosphatase, and is more similar to human NUDT9. The latter observation provided new insights into the ligand binding mode of ADPR-gated Ca2+ channel TRPM2.

PubMed: 18275811
DOI: 10.1016/j.str.2007.11.017

実験手法

X-RAY DIFFRACTION (2.6 Å)