3zu0 | pdb_00003zu0

Structure of Haemophilus influenzae NAD nucleotidase (NadN)

spinqualitylabelsall models 3zu0, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3zu0 is a 2 chain structure with sequence from Haemophilus influenzae Rd KW20. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.001Å Ligands: A12, PO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 5NTD_HAEIN Degrades NAD into adenosine and nicotinamide riboside, the latter being subsequently internalized by a specific permease. Also endowed with NAD(P) pyrophosphatase activity. Exhibits a broad substrate specificity, recognizing either mono- or dinucleotide nicotinamides and different adenosine phosphates with a maximal activity on 5'-adenosine monophosphate. Publication Abstract from PubMed Haemophilus influenzae is a major pathogen of the respiratory tract in humans that has developed the capability to exploit host NAD(P) for its pyridine dinucleotide requirement. This strategy is organized around a periplasmic enzyme termed NadN, that plays a central role by degrading NAD into adenine and nicotinamide riboside, the latter being subsequently internalized by a specific permease. We performed a biochemical and structural investigation on H. influenzae NadN that determined the enzyme is a Zn2+-dependent 5'-nucleotidase also endowed with NAD(P) pyrophosphatase activity. A 1.3 A resolution structural analysis revealed a remarkable conformational change that occurs during catalysis between the open and closed forms of the enzyme. NadN showed a broad substrate specificity recognizing either mono or dinucleotide pyridines and different adenosine phosphates with a maximal activity on 5' adenosine monophosphate. Sequence and structural analysis of H. influenzae NadN led us to discover that human CD73 is capable of processing both NAD and NMN, therefore disclosing a possible novel function of human CD73 in systemic NAD metabolism. Our data may prove to be useful for inhibitor design and disclosed unanticipated fascinating evolutionary relationships. The high-resolution crystal structure of periplasmic Haemophilus influenzae NAD nucleotidase reveals a novel enzymatic function of human CD73 related to NAD metabolism.,Garavaglia S, Bruzzone S, Cassani C, Canella L, Allegrone G, Sturla L, Mannino E, Millo E, De Flora A, Rizzi M Biochem J. 2011 Sep 20. PMID:21933152 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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