› 2jfs

X-ray diffraction
1.45Å resolution

Crystal structure of the PPM Ser-Thr phosphatase MsPP from Mycobacterium smegmatis in complex with cacodylate

Released:
DOI: 10.2210/pdb2jfs/pdb
PDB entry 2jfs coloured by chain, front view.
PDB entry 2jfs coloured by chain, side view.
PDB entry 2jfs coloured by chain, top view.
Source organism: Mycolicibacterium smegmatis MC2 155
Primary publication:
Insights into the catalytic mechanism of PPM Ser/Thr phosphatases from the atomic resolution structures of a mycobacterial enzyme.
Bellinzoni M, Wehenkel A, Shepard W, Alzari PM
Structure 15 863-72 (2007)
PMID: 17637345

Function and Biology Details

Reaction catalysed: 
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106315 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
protein-serine/threonine phosphatase Chain: A
Molecule details ›
Chain: A
Length: 234 amino acids
Theoretical weight: 24.28 KDa
Source organism: Mycolicibacterium smegmatis MC2 155
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0QTQ6 (Residues: 1-233; Coverage: 100%)
Gene name: MSMEG_1928
Sequence domains: Protein phosphatase 2C
Structure domains: PPM-type phosphatase domain

Ligands and Environments

3 bound ligands:
Ligand MN 3 x MN
Ligand CAC 1 x CAC
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 36.568Å b: 65.786Å c: 110.059Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.178 0.191
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Serine/threonine phosphatases: mechanism through structure.
Shi Y. (2009)
2 more

2 mentions without citation

Structural basis for Rab1 de-AMPylation by the Legionella pneumophila effector SidD.
Chen et al. (2013)
1 more