2JGR

Crystal structure of YegS in complex with ADP

2JGR の概要

• エントリーDOI: 10.2210/pdb2jgr/pdb
• 関連するPDBエントリー: 2BON
• 分子名称: YEGS, PYROPHOSPHATE 2- (3 entities in total)
• 機能のキーワード: phosphatidylglycerole kinase, transferase, lipid kinase, pyrrophosphate, hypothetical protein
• 由来する生物種: ESCHERICHIA COLI
• 細胞内の位置: Cytoplasm: P76407
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32570.75

構造登録者

Bakali, H.M.,Herman, M.D.,Johnson, K.A.,Kelly, A.A.,Wieslander, A.,Hallberg, B.M.,Nordlund, P. (登録日: 2007-02-14, 公開日: 2007-05-15, 最終更新日: 2024-10-23)

主引用文献

Bakali, H.M.,Herman, M.D.,Johnson, K.A.,Kelly, A.A.,Wieslander, A.,Hallberg, B.M.,Nordlund, P.
Crystal Structure of Yegs, a Homologue to the Mammalian Diacylglycerol Kinases, Reveals a Novel Regulatory Metal Binding Site.
J.Biol.Chem., 282:19644-, 2007

PubMed Abstract: The human lipid kinase family controls cell proliferation, differentiation, and tumorigenesis and includes diacylglycerol kinases, sphingosine kinases, and ceramide kinases. YegS is an Escherichia coli protein with significant sequence homology to the catalytic domain of the human lipid kinases. We have solved the crystal structure of YegS and shown that it is a lipid kinase with phosphatidylglycerol kinase activity. The crystal structure reveals a two-domain protein with significant structural similarity to a family of NAD kinases. The active site is located in the interdomain cleft formed by four conserved sequence motifs. Surprisingly, the structure reveals a novel metal binding site composed of residues conserved in most lipid kinases.

PubMed: 17351295
DOI: 10.1074/JBC.M604852200

実験手法

X-RAY DIFFRACTION (2.65 Å)