1PYM

PHOSPHOENOLPYRUVATE MUTASE FROM MOLLUSK IN WITH BOUND MG2-OXALATE

Summary for 1PYM

• Entry DOI: 10.2210/pdb1pym/pdb
• Descriptor: PROTEIN (PHOSPHOENOLPYRUVATE MUTASE), OXALATE ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: phosphotransferase, phosphomutase, p-c bond formation
• Biological source: Mytilus edulis
• Total number of polymer chains: 2
• Total formula weight: 66789.87

Authors

Huang, K.,Li, Z.,Herzberg, O. (deposition date: 1999-02-25, release date: 1999-07-21, Last modification date: 2024-11-06)

Primary citation

Huang, K.,Li, Z.,Jia, Y.,Dunaway-Mariano, D.,Herzberg, O.
Helix swapping between two alpha/beta barrels: crystal structure of phosphoenolpyruvate mutase with bound Mg(2+)-oxalate.
Structure Fold.Des., 7:539-548, 1999

PubMed Abstract: Phosphonate compounds are important secondary metabolites in nature and, when linked to macromolecules in eukaryotes, they might play a role in cell signaling. The first obligatory step in the biosynthesis of phosphonates is the formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-pyr), a reaction that is catalyzed by PEP mutase. The PEP mutase functions as a tetramer and requires magnesium ions (Mg2+).

PubMed: 10378273
DOI: 10.1016/S0969-2126(99)80070-7

Experimental method

X-RAY DIFFRACTION (1.8 Å)