› 2je5

X-ray diffraction
2.6Å resolution

STRUCTURAL AND MECHANISTIC BASIS OF PENICILLIN BINDING PROTEIN INHIBITION BY LACTIVICINS

Released:
DOI: 10.2210/pdb2je5/pdb
PDB entry 2je5 coloured by chain, front view.
PDB entry 2je5 coloured by chain, side view.
PDB entry 2je5 coloured by chain, top view.
Source organism: Streptococcus pneumoniae R6
Primary publication:
Structural and mechanistic basis of penicillin-binding protein inhibition by lactivicins.
Macheboeuf P, Fischer DS, Brown T, Zervosen A, Luxen A, Joris B, Dessen A, Schofield CJ
Nat Chem Biol 3 565-9 (2007)
PMID: 17676039

Function and Biology Details

Reaction catalysed: 
(GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl diphosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130673 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
peptidoglycan glycosyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 720 amino acids
Theoretical weight: 78.43 KDa
Source organism: Streptococcus pneumoniae R6
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O70038 (Residues: 72-791; Coverage: 88%)
Gene name: pbp1b
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand L4C 2 x L4C
Ligand SO4 2 x SO4
Ligand CL 4 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 98.54Å b: 99.83Å c: 152.16Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.262 0.26 0.298
Expression system: Escherichia coli BL21

Quick links

Citations

17 review citations

Electrophilic natural products and their biological targets.
Gersch et al. (2012)
16 more

1 mention without citation

Utilization of protein intrinsic disorder knowledge in structural proteomics.
Oldfield et al. (2013)