ArticlePloS one2015
Structural and enzymatic characterization of the choline kinase LicA from Streptococcus pneumoniae.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Kaempferol activity onPharmaceutical biology · 2026Article
- Biosynthesis of mitis group streptococcal glycolipids and their roles in physiology and antibiotic susceptibility.bioRxiv : the preprint server for biology · 2024Article
- Structure and kinase activity of bacterial cell cycle regulator CcrZ.PLoS genetics · 2022Article
- Mechanistic basis of choline import involved in teichoic acids and lipopolysaccharide modification.Science advances · 2022Article
- CcrZ is a pneumococcal spatiotemporal cell cycle regulator that interacts with FtsZ and controls DNA replication by modulating the activity of DnaA.Nature microbiology · 2021Article
- ChoK-ing the Pathogenic Bacteria: Potential of Human Choline Kinase Inhibitors as Antimicrobial Agents.BioMed research international · 2020Review
- Choline Kinase Emerges as a Promising Drug Target in Gram-Positive Bacteria.Frontiers in microbiology · 2019Article
- Parallel Colorimetric Quantification of Choline and Phosphocholine as a Method for Studying Choline Kinase Activity in Complex Mixtures.Antibiotics (Basel, Switzerland) · 2018Article
- Choline Kinase, A Novel Drug Target for the Inhibition of Streptococcus pneumoniae.Antibiotics (Basel, Switzerland) · 2017Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
LicA plays a key role in the cell-wall phosphorylcholine biosynthesis of Streptococcus pneumonia. Here we determined the crystal structures of apo-form LicA at 1.94 Å and two complex forms LicA-choline and LicA-AMP-MES, at 2.01 and 1.45 Å resolution, respectively. The overall structure adopts a canonical protein kinase-like fold, with the active site located in the crevice of the N- and C-terminal domains. The three structures present distinct poses of the active site, which undergoes an open-closed-open conformational change upon substrate binding and product release. The structure analyses combined with mutageneses and enzymatic assays enabled us to figure out the key residues for the choline kinase activity of LicA. In addition, structural comparison revealed the loop between helices α7 and α8 might modulate the substrate specificity and catalytic activity. These findings shed light on the structure and mechanism of the prokaryotic choline kinase LicA, and might direct the rational design of novel anti-pneumococcal drugs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.