3CR3

Structure of a transient complex between Dha-kinase subunits DhaM and DhaL from Lactococcus lactis

Summary for 3CR3

• Entry DOI: 10.2210/pdb3cr3/pdb
• Related: 2BTD 2IU4 2IU5 2IU6
• Descriptor: PTS-dependent dihydroxyacetone kinase, ADP-binding subunit dhaL, PTS-dependent dihydroxyacetone kinase, phosphotransferase subunit dhaM, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: transient protein-protein complex transferase complex pts-dependent dihydroxyacetone kinase, atp-binding, glycerol metabolism, nucleotide-binding, phosphotransferase system, transferase
• Biological source: Lactococcus lactis subsp. lactis (Streptococcus lactis); More
• Total number of polymer chains: 4
• Total formula weight: 69492.10

Authors

Jeckelmann, J.M.,Zurbriggen, A.,Christen, S.,Baumann, U.,Erni, B. (deposition date: 2008-04-04, release date: 2008-10-21, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)