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Enzyme–ligand interactions that drive active site rearrangements in the Helicobacter pylori 5′-methylthioadenosine/S-adenosylhomocysteine nucleosidase by Donald R. Ronning; Natalie M. Iacopelli; Vidhi Mishra is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Enzyme–ligand interactions that drive active site rearrangements in the Helicobacter pylori 5′-methylthioadenosine/S-adenosylhomocysteine nucleosidase about?

## Abstract 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 Å, respectively. The ribose‐binding site in the MTAN and MTAN‐adenine cocrystal 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

Who reads Enzyme–ligand interactions that drive active site rearrangements in the Helicobacter pylori 5′-methylthioadenosine/S-adenosylhomocysteine nucleosidase?

Author

Donald R. Ronning; Natalie M. Iacopelli; Vidhi Mishra

Publisher

Cold Spring Harbor Laboratory Press; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley (ISSN 0961-8368)

Published

2010

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)