4r78 | pdb_00004r78

Crystal structure of LicA in complex with AMP

spinqualitylabelsall models 4r78, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4r78 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AMP, MES Related: 4r77, 4r7b Activity: Choline kinase, with EC number 2.7.1.32 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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 A and two complex forms LicA-choline and LicA-AMP-MES, at 2.01 and 1.45 A 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 alpha7 and alpha8 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. Structural and enzymatic characterization of the choline kinase LicA from Streptococcus pneumoniae.,Wang L, Jiang YL, Zhang JR, Zhou CZ, Chen Y PLoS One. 2015 Mar 17;10(3):e0120467. doi: 10.1371/journal.pone.0120467., eCollection 2015. PMID:25781969 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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