› 3w43

X-ray diffraction
1.22Å resolution

Crystal structure of RsbX in complex with manganese in space group P21

Released:
DOI: 10.2210/pdb3w43/pdb
PDB entry 3w43 coloured by chain, front view.
PDB entry 3w43 coloured by chain, side view.
PDB entry 3w43 coloured by chain, top view.
Source organism: Bacillus subtilis subsp. subtilis str. 168
Primary publication:
Structure of the RsbX phosphatase involved in the general stress response of Bacillus subtilis.
Teh AH, Makino M, Hoshino T, Baba S, Shimizu N, Yamamoto M, Kumasaka T
Acta Crystallogr D Biol Crystallogr 71 1392-9 (2015)
PMID: 26057679

Function and Biology Details

Reaction catalysed: 
O-phospho-L(or D)-serine + H(2)O = L(or D)-serine + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148212 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoserine phosphatase RsbX Chain: A
Molecule details ›
Chain: A
Length: 199 amino acids
Theoretical weight: 22.17 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli
UniProt:
  • Canonical: P17906 (Residues: 1-199; Coverage: 100%)
Gene names: BSU04740, rsbX
Sequence domains: Stage II sporulation protein E (SpoIIE)
Structure domains: PPM-type phosphatase domain

Ligands and Environments

1 bound ligand:
Ligand MN 2 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P21
Unit cell:
a: 40.858Å b: 48.925Å c: 44.607Å
α: 90° β: 93.61° γ: 90°
R-values:
R R work R free
0.158 0.156 0.189
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Conformational Changes in Active and Inactive States of Human PP2Cα Characterized by Hydrogen/Deuterium Exchange-Mass Spectrometry.
Mazur et al. (2017)
4 more

1 mention without citation

A widespread family of serine/threonine protein phosphatases shares a common regulatory switch with proteasomal proteases.
Bradshaw et al. (2017)