Phosphorylated beta-phosphoglucomutase from Lactococcus lactis in an open conformer to 2.4 A

Transition state of phospho-enzyme hydrolysis in beta-phosphoglucomutase

Residue D8 is modified by phosphorylation in the pre-formed crystal.

MFKAVLF(PHD)LDGVITDTAEYHFRAWKALAEEIGINGVDRQFNEQLKGVSREDSLQKILDLADKKVSAEEFKELAKRK
NDNYVKMIQDVSPADVYPGILQLLKDLRSNKIKIALASASKNGPFLLERMNLTGYFDAIADPAEVAASKPAPDIFIAAAH
AVGVAPSESIGLEDSQAGIQAIKDSGALPIGVGRPEDLGDDIVIVPDTSHYTLEFLKEVWLQKQK

MFKAVLFDLDGVITDTAEYHFRAWKALAEEIGINGVDRQFNEQLKGVSREDSLQKILDLADKKVSAEEFKELAKRKNDNY
VKMIQDVSPADVYPGILQLLKDLRSNKIKIALASASKNGPFLLERMNLTGYFDAIADPAEVAASKPAPDIFIAAAHAVGV
APSESIGLEDSQAGIQAIKDSGALPIGVGRPEDLGDDIVIVPDTSHYTLEFLKEVWLQKQK

24-34% PEG 4000,
200 mM sodium acetate,
50 mM TRIS pH 7.5,

The crystal was cryoprotected in its original mother liquor plus an additional 25% ethylene glycol and 30mM acetylphosphate.

Biotechnology and Biological Sciences Research Council

Solution Nuclear Magnetic Resonance data of PGM incubated with acetylphosphate demonstrates that phospho-enzyme is formed as is presented in the crystal structure.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

phosphoglucomutase, isomerase, phospho-enzyme, acetylphosphate

MFKAVLFDLDGVITDTAEYHFRAWKALAEEIGINGVDRQFNEQLKGVSREDSLQKILDLADKKVSAEEFKELAKRKNDNY
VKMIQDVSPADVYPGILQLLKDLRSNKIKIALASASKNGPFLLEKMNLTGYFDAIADPAEVAASKPAPDIFIAAAHAVGV
APSESIGLEDSQAGIQAIKDSGALPIGVGRPEDLGDDIVIVPDTSYYTLEFLKEVWLQKQK