3nm4 | pdb_00003nm4

Helicobacter pylori MTAN

spinqualitylabelsall models 3nm4, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3nm4 is a 2 chain structure with sequence from Campylobacter pylori j99. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, TRS Related: 3nm5, 3nm6 Gene: jhp_0082, mtn, mtnN, Pfs (Campylobacter pylori J99) Activity: Adenosylhomocysteine nucleosidase, with EC number 3.2.2.9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MTNN_HELPJ] Responsible for cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH) (By similarity). Publication Abstract from PubMed The bacterial enzyme 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (MTAN) plays a central role in three essential metabolic pathways in bacteria: methionine salvage, purine salvage, and polyamine biosynthesis. Recently, its role in the pathway that leads to the production of autoinducer II, an important component in quorum-sensing, has garnered much interest. Because of this variety of roles, MTAN is an attractive target for developing new classes of inhibitors that influence bacterial virulence and biofilm formation. To gain insight toward the development of new classes of MTAN inhibitors, the interactions between the Helicobacter pylori encoded MTAN and its substrates and substrate analogs were probed using X-ray crystallography. The structures of MTAN, an MTAN-Formycin A complex, and an adenine bound form were solved by molecular replacement and refined to 1.7, 1.8, and 1.6 A, respectively. The ribose binding site in the MTAN and MTAN-adenine co-crystal structures contain a tris[hydroxymethyl]aminomethane molecule, that stabilizes the closed form of the enzyme and displaces a nucleophilic water molecule necessary for catalysis. This research gives insight to the interactions between MTAN and bound ligands that promote closing of the enzyme active site and highlights the potential for designing new classes of MTAN inhibitors using a link/grow or ligand assembly development strategy based on the described H. pylori MTAN crystal structures. Enzyme-ligand interactions that drive active site rearrangements in the Helicobacter pylori 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase.,Ronning DR, Iacopelli NM, Mishra V Protein Sci. 2010 Oct 15. PMID:20954236 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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