4R7B

Crystal structure of pneumococcal LicA in complex with choline

4R7B の概要

• エントリーDOI: 10.2210/pdb4r7b/pdb
• 関連するPDBエントリー: 4R77 4R78
• 分子名称: Choline kinase, CHOLINE ION (3 entities in total)
• 機能のキーワード: protein kinase-like fold, transferase
• 由来する生物種: Streptococcus pneumoniae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 71430.08

構造登録者

Wang, L.,Jiang, Y.L.,Zhou, C.Z.,Chen, Y.X. (登録日: 2014-08-27, 公開日: 2015-08-12, 最終更新日: 2023-11-08)

主引用文献

Wang, L.,Jiang, Y.L.,Zhang, J.R.,Zhou, C.Z.,Chen, Y.X.
Structural and enzymatic characterization of the choline kinase LicA from Streptococcus pneumoniae
Plos One, 10:e0120467-e0120467, 2015

PubMed 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.

PubMed: 25781969
DOI: 10.1371/journal.pone.0120467

実験手法

X-RAY DIFFRACTION (2.01 Å)