› 2z8m

X-ray diffraction
2Å resolution

Structural basis for the catalytic mechanism of phosphothreonine lyase

Released:
DOI: 10.2210/pdb2z8m/pdb
PDB entry 2z8m coloured by chain, front view.
PDB entry 2z8m coloured by chain, side view.
PDB entry 2z8m coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-141066 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
MAPK phosphothreonine lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 241 amino acids
Theoretical weight: 27.68 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

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 64.49Å b: 71.95Å c: 106.27Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.23
Expression system: Escherichia coli BL21

Quick links

Citations

13 review citations

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

1 mention without citation

Genome-wide search for eliminylating domains reveals novel function for BLES03-like proteins.
Khater et al. (2014)