PMID:25781969

Citation	Wang, L, Jiang, YL, Zhang, JR, Zhou, CZ and Chen, Y (2015) Structural and Enzymatic Characterization of the Choline Kinase LicA from Streptococcus pneumoniae. PLoS ONE 10:e0120467
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.
Links	PubMed PMC4364537 Online version:10.1371/journal.pone.0120467
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
STREE:Q93MI3		GO:0004103: choline kinase activity	ECO:0000315:		F		Figure 4B shows that wild-type LicA phosphorylates choline, and mutations in the proposed critical residues drastically decreases the ability of LicA to phosphorylate choline.	complete CACAO 10931
STREE:Q93MI3	enables	GO:0004103: choline kinase activity	ECO:0000315: mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete

References

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