2QJO: Crystal Structure Of A Bifunctional Nmn Adenylyltransferase/adp Ribose Pyrophosphatase (nadm) Complexed With Adprp And Nad From Synechocystis Sp

Citation:
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.
PDB ID: 2QJODownload
MMDB ID: 62919
PDB Deposition Date: 2007/7/8
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.6  Å
Source Organism:
Similar Structures:
Biological Unit for 2QJO: hexameric; determined by author and by software (PISA,PQS)
Molecular Components in 2QJO
Label Count Molecule
Proteins (6 molecules)
6
Bifunctional NMN Adenylyltransferase/nudix Hydrolase
Molecule annotation
Chemicals (26 molecules)
1
8
2
6
3
6
4
6
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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