› 2huc

X-ray diffraction
1.9Å resolution

Structural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Protein Variants

Released:
DOI: 10.2210/pdb2huc/pdb
PDB entry 2huc coloured by chain, front view.
PDB entry 2huc coloured by chain, side view.
PDB entry 2huc coloured by chain, top view.
Source organism: Bacillus cereus
Primary publication:
Structural studies examining the substrate specificity profiles of PC-PLC(Bc) protein variants.
Benfield AP, Goodey NM, Phillips LT, Martin SF
Arch Biochem Biophys 460 41-7 (2007)
PMID: 17324372

Function and Biology Details

Reaction catalysed: 
A phosphatidylcholine + H(2)O = 1,2-diacyl-sn-glycerol + phosphocholine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140704 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipase C Chain: A
Molecule details ›
Chain: A
Length: 245 amino acids
Theoretical weight: 28.35 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli
UniProt:
  • Canonical: P09598 (Residues: 39-283; Coverage: 95%)
Gene name: plc
Sequence domains: Zinc dependent phospholipase C
Structure domains: P1 Nuclease

Ligands and Environments

1 bound ligand:
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43212
Unit cell:
a: 89.973Å b: 89.973Å c: 71.957Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.187 0.208
Expression system: Escherichia coli

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Citations

3 review citations

Bacillus thuringiensis membrane-damaging toxins acting on mammalian cells.
Celandroni et al. (2014)
2 more

3 mentions without citation

Structural studies examining the substrate specificity profiles of PC-PLC(Bc) protein variants.
Benfield et al. (2007)
2 more