2JFT: Crystal Structure Of The Ppm Ser-thr Phosphatase Mspp From Mycobacterium Smegmatis In Complex With Sulfate

Serine/threonine-specific phosphatases (PPs) represent, after protein tyrosine phosphatases, the second major class of enzymes that catalyze the dephosphorylation of proteins. They are classed in two large families, known as PPP and PPM, on the basis of sequence similarities, metal ion dependence, and inhibitor sensitivity. Despite their wide species distribution and broad physiological roles, the catalytic mechanism of PPM phosphatases has been primarily inferred from studies of a single enzyme, human PP2Calpha. Here, we report the biochemical characterization and the atomic resolution structures of a soluble PPM phosphatase from the saprophyte Mycobacterium smegmatis in complex with different ligands. The structures provide putative snapshots along the catalytic cycle, which support an associative reaction mechanism that differs in some important aspects from the currently accepted model and reinforces the hypothesis of convergent evolution in PPs.
PDB ID: 2JFTDownload
MMDB ID: 53776
PDB Deposition Date: 2007/2/4
Updated in MMDB: 2012/10
Experimental Method:
x-ray diffraction
Resolution: 1.08  Å
Source Organism:
Similar Structures:
Biological Unit for 2JFT: monomeric; determined by author and by software (PQS)
Molecular Components in 2JFT
Label Count Molecule
Protein (1 molecule)
Ser-thr Phosphatase Mspp
Molecule annotation
Chemicals (7 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB