› 6h8n

X-ray diffraction
1.26Å resolution

Structure of peptidoglycan deacetylase PdaC from Bacillus subtilis - mutant D285S

Released:
DOI: 10.2210/pdb6h8n/pdb
PDB entry 6h8n coloured by chain, front view.
PDB entry 6h8n coloured by chain, side view.
PDB entry 6h8n coloured by chain, top view.
Source organism: Bacillus subtilis subsp. subtilis str. 168
Primary publication:
Structure-function relationships underlying the dual N-acetylmuramic and N-acetylglucosamine specificities of the bacterial peptidoglycan deacetylase PdaC.
Grifoll-Romero L, Sainz-Polo MA, Albesa-Jové D, Guerin ME, Biarnés X, Planas A
J Biol Chem 294 19066-19080 (2019)
PMID: 31690626

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128600 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidoglycan-N-acetylmuramic acid deacetylase PdaC Chains: A, B
Molecule details ›
Chains: A, B
Length: 212 amino acids
Theoretical weight: 24.49 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O34798 (Residues: 270-467; Coverage: 42%)
Gene names: BSU12100, pdaC, yjeA
Sequence domains: Polysaccharide deacetylase

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand PO4 3 x PO4
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 55.42Å b: 61.8Å c: 130.99Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.16 0.174
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Resistance Mechanisms to Antimicrobial Peptides in Gram-Positive Bacteria.
Assoni et al. (2020)
1 more

1 mention without citation

Structure-function relationships underlying the dual N-acetylmuramic and N-acetylglucosamine specificities of the bacterial peptidoglycan deacetylase PdaC.
Grifoll-Romero et al. (2019)