ArticlePloS one2012
Structures of Helicobacter pylori shikimate kinase reveal a selective inhibitor-induced-fit mechanism.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 34 citations in OpenAlex.
- Computational investigation of African natural products as Helicobacter pylori shikimate kinase inhibitors.PloS one · 2026Article
- Repurposing FDA-Approved Agents to Develop a PrototypePharmaceuticals (Basel, Switzerland) · 2025Article
- TargetingFrontiers in cellular and infection microbiology · 2025Article
- Inhibition of Shikimate Kinase from Methicillin-ResistantInternational journal of molecular sciences · 2024Article
- Multiple Metabolic Engineering Strategies to Improve Shikimate Titer inMetabolites · 2023Article
- Molecular analysis and essentiality of Aro1 shikimate biosynthesis multi-enzyme inLife science alliance · 2022Article
- Review
- In Silico and In Vitro Anti-Molecules (Basel, Switzerland) · 2019Article
- Biochemical, Kinetic, and Computational Structural Characterization of Shikimate Kinase from Methicillin-Resistant Staphylococcus aureus.Molecular biotechnology · 2019Article
- Non-pharmacological treatment of Helicobacter pylori.World journal of gastrointestinal pharmacology and therapeutics · 2016Review
- Detection of trans-cis flips and peptide-plane flips in protein structures.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Elevated levels of adaption in Helicobacter pylori genomes from Japan; a link to higher incidences of gastric cancer?Evolution, medicine, and public health · 2015Article
- Utility of the Biosynthetic Folate Pathway for Targets in Antimicrobial Discovery.Antibiotics (Basel, Switzerland) · 2014Review
- Pathway-based screening strategy for multitarget inhibitors of diverse proteins in metabolic pathways.PLoS computational biology · 2013Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Shikimate kinase (SK), which catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid in the presence of ATP, is the enzyme in the fifth step of the shikimate pathway for biosynthesis of aromatic amino acids. This pathway is present in bacteria, fungi, and plants but absent in mammals and therefore represents an attractive target pathway for the development of new antimicrobial agents, herbicides, and antiparasitic agents. Here we investigated the detailed structure-activity relationship of SK from Helicobacter pylori (HpSK). Site-directed mutagenesis and isothermal titration calorimetry studies revealed critical conserved residues (D33, F48, R57, R116, and R132) that interact with shikimate and are therefore involved in catalysis. Crystal structures of HpSK·SO(4), R57A, and HpSK•shikimate-3-phosphate • ADP show a characteristic three-layer architecture and a conformationally elastic region consisting of F48, R57, R116, and R132, occupied by shikimate. The structure of the inhibitor complex, E114A • 162535, was also determined, which revealed a dramatic shift in the elastic LID region and resulted in conformational locking into a distinctive form. These results reveal considerable insight into the active-site chemistry of SKs and a selective inhibitor-induced-fit mechanism.
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