› 5jip

X-ray diffraction
1.8Å resolution

Crystal structure of the Clostridium perfringens spore cortex lytic enzyme SleM

Released:
DOI: 10.2210/pdb5jip/pdb
PDB entry 5jip coloured by chain, front view.
PDB entry 5jip coloured by chain, side view.
PDB entry 5jip coloured by chain, top view.
Source organism: Clostridium perfringens
Primary publication:
The crystal structure of Clostridium perfringens SleM, a muramidase involved in cortical hydrolysis during spore germination.
Al-Riyami B, Üstok FI, Stott K, Chirgadze DY, Christie G
Proteins 84 1681-1689 (2016)
PMID: 27488615

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Muramidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 332 amino acids
Theoretical weight: 37.58 KDa
Source organism: Clostridium perfringens
Expression system: Escherichia coli
UniProt:
  • Canonical: O06496 (Residues: 2-321; Coverage: 100%)
Gene names: EHZ11_04715, NCTC10719_02777, acm, sleM
Sequence domains: Glycosyl hydrolases family 25
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MES 4 x MES
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P21
Unit cell:
a: 50.599Å b: 85.852Å c: 87.205Å
α: 90° β: 105.51° γ: 90°
R-values:
R R work R free
0.153 0.151 0.182
Expression system: Escherichia coli

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Citations

1 review citation

Germination of Spores of the Orders Bacillales and Clostridiales.
Setlow et al. (2017)
2 other articles

3 mentions without citation

Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan.
Vermassen et al. (2019)
2 more