2QJO

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

Summary for 2QJO

• Entry DOI: 10.2210/pdb2qjo/pdb
• Descriptor: Bifunctional NMN adenylyltransferase/Nudix hydrolase, SULFATE ION, ADENOSINE-5-DIPHOSPHORIBOSE, ... (6 entities in total)
• Functional Keywords: two individual domains, transferase, hydrolase
• Biological source: Synechocystis sp.
• Cellular location: Cytoplasm : Q55928
• Total number of polymer chains: 3
• Total formula weight: 120951.21

Authors

Huang, N.,Sorci, L.,Zhang, X.,Brautigan, C.,Raffaelli, N.,Magni, G.,Grishin, N.V.,Osterman, A.,Zhang, H. (deposition date: 2007-07-08, release date: 2008-03-11, Last modification date: 2024-02-21)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)