ArticleProtein science : a publication of the Protein Society2010
Enzyme-ligand interactions that drive active site rearrangements in the Helicobacter pylori 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 31 citations in OpenAlex.
- GC-MS Profiling, Anti-Plants (Basel, Switzerland) · 2022Article
- Chemoenzymatic labeling of DNA methylation patterns for single-molecule epigenetic mapping.Nucleic acids research · 2022Article
- SAXS Analysis and Characterization of Anticancer Activity of PNP-UDP Family Protein from Putranjiva roxburghii.The protein journal · 2022Article
- Identification of immucillin analogue natural compounds to inhibitIn silico pharmacology · 2021Article
- Transition State Analogues Enhanced by Fragment-Based Structural Analysis: Bacterial Methylthioadenosine Nucleosidases.Biochemistry · 2020Article
- Selective Inhibitors of Helicobacter pylori Methylthioadenosine Nucleosidase and Human Methylthioadenosine Phosphorylase.Journal of medicinal chemistry · 2019Article
- Enzymatic Transition States and Drug Design.Chemical reviews · 2018Review
- Transition-State Analogues of Campylobacter jejuni 5'-Methylthioadenosine Nucleosidase.ACS chemical biology · 2018Article
- Interference With Quorum-Sensing Signal Biosynthesis as a Promising Therapeutic Strategy Against Multidrug-Resistant Pathogens.Frontiers in cellular and infection microbiology · 2018Review
- Neutron structures of the Helicobacter pylori 5'-methylthioadenosine nucleosidase highlight proton sharing and protonation states.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Transition State Structure and Inhibition of Rv0091, a 5'-Deoxyadenosine/5'-methylthioadenosine Nucleosidase from Mycobacterium tuberculosis.ACS chemical biology · 2016Article
- Molecular dynamics study of the effect of active site protonation on Helicobacter pylori 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase.European biophysics journal : EBJ · 2015Article
- Crystallization and preliminary X-ray diffraction analysis of the interaction of Aeromonas hydrophila MtaN-1 with S-adenosylhomocysteine.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Structural and biochemical characterization of Chlamydia trachomatis hypothetical protein CT263 supports that menaquinone synthesis occurs through the futalosine pathway.The Journal of biological chemistry · 2014Article
- Salmonella enterica MTAN at 1.36 Å resolution: a structure-based design of tailored transition state analogs.Structure (London, England : 1993) · 2013Article
- Crystal structures of the Helicobacter pylori MTAN enzyme reveal specific interactions between S-adenosylhomocysteine and the 5'-alkylthio binding subsite.Biochemistry · 2012Article
- Small molecule control of bacterial biofilms.Organic & biomolecular chemistry · 2012Review
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3 authors at 1 institution in 1 country.
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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 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.
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