› 2z8p

X-ray diffraction
1.8Å resolution

Structural basis for the catalytic mechanism of phosphothreonine lyase

Released:
DOI: 10.2210/pdb2z8p/pdb
PDB entry 2z8p coloured by chain, front view.
PDB entry 2z8p coloured by chain, side view.
PDB entry 2z8p coloured by chain, top view.
Source organisms:
Primary publication:
Structural basis for the catalytic mechanism of phosphothreonine lyase.
Chen L, Wang H, Zhang J, Gu L, Huang N, Zhou JM, Chai J
Nat Struct Mol Biol 15 101-2 (2008)
PMID: 18084305

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141067 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
MAPK phosphothreonine lyase Chain: A
Molecule details ›
Chain: A
Length: 241 amino acids
Theoretical weight: 27.62 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0A2M9 (Residues: 1-241; Coverage: 100%)
Gene names: PSLT038, mkaD, spvC, vsdD
Sequence domains: Salmonella virulence-associated 28kDa protein
Structure domains: phosphothreonine lyase
(GLY)(GLU)(ALA)(TPO)(VAL)(PTR)(ALA) Chain: B
Molecule details ›
Chain: B
Length: 7 amino acids
Theoretical weight: 870 Da
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
2 modified residues:
Ligand TPO 1 x TPO
Ligand PTR 1 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 37.31Å b: 71.42Å c: 98.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.211 0.229
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

12 review citations

Histone modifications and chromatin remodeling during bacterial infections.
Hamon et al. (2008)
11 more

4 mentions without citation

Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes.
Repka et al. (2017)
3 more