3CT6

Crystal structure of DhaM of L. lactis

3CT6 の概要

• エントリーDOI: 10.2210/pdb3ct6/pdb
• 分子名称: PTS-dependent dihydroxyacetone kinase, phosphotransferase subunit dhaM (2 entities in total)
• 機能のキーワード: mixed alpha beta structure, glycerol metabolism, kinase, phosphotransferase system, transferase
• 由来する生物種: Lactococcus lactis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28956.94

構造登録者

Zurbriggen, A. (登録日: 2008-04-11, 公開日: 2008-10-21, 最終更新日: 2024-02-21)

主引用文献

Zurbriggen, A.,Jeckelmann, J.M.,Christen, S.,Bieniossek, C.,Baumann, U.,Erni, B.
X-ray Structures of the Three Lactococcus lactis Dihydroxyacetone Kinase Subunits and of a Transient Intersubunit Complex.
J.Biol.Chem., 283:35789-35796, 2008

PubMed Abstract: Bacterial dihydroxyacetone (Dha) kinases do not exchange the ADP for ATP but utilize a subunit of the phosphoenolpyruvate carbohydrate phosphotransferase system for in situ rephosphorylation of a permanently bound ADP-cofactor. Here we report the 2.1-angstroms crystal structure of the transient complex between the phosphotransferase subunit DhaM of the phosphotransferase system and the nucleotide binding subunit DhaL of the Dha kinase of Lactococcus lactis, the 1.1-angstroms structure of the free DhaM dimer, and the 2.5-angstroms structure of the Dha-binding DhaK subunit. Conserved salt bridges and an edge-to-plane stacking contact between two tyrosines serve to orient DhaL relative to the DhaM dimer. The distance between the imidazole Nepsilon2 of the DhaM His-10 and the beta-phosphate oxygen of ADP, between which the gamma-phosphate is transferred, is 4.9 angstroms. An invariant arginine, which is essential for activity, is appropriately positioned to stabilize the gamma-phosphate in the transition state. The (betaalpha)4alpha fold of DhaM occurs a second time as a subfold in the DhaK subunit. By docking DhaL-ADP to this subfold, the nucleotide bound to DhaL and the C1-hydroxyl of Dha bound to DhaK are positioned for in-line transfer of phosphate.

PubMed: 18957416
DOI: 10.1074/jbc.M804893200

実験手法

X-RAY DIFFRACTION (1.1 Å)