› 1k25

X-ray diffraction
3.2Å resolution

PBP2x from a Highly Penicillin-resistant Streptococcus pneumoniae Clinical Isolate

Released:
DOI: 10.2210/pdb1k25/pdb
PDB entry 1k25 coloured by chain, front view.
PDB entry 1k25 coloured by chain, side view.
PDB entry 1k25 coloured by chain, top view.
Source organism: Streptococcus pneumoniae
Primary publication:
Crystal structure of PBP2x from a highly penicillin-resistant Streptococcus pneumoniae clinical isolate: a mosaic framework containing 83 mutations.
Dessen A, Mouz N, Gordon E, Hopkins J, Dideberg O
J Biol Chem 276 45106-12 (2001)
PMID: 11553637

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128516 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PASTA domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 685 amino acids
Theoretical weight: 75.26 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: O34006 (Residues: 66-750; Coverage: 91%)
Gene name: pbp2X
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P32
Unit cell:
a: 146.56Å b: 146.56Å c: 132.61Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.235 0.235 0.312
Expression system: Escherichia coli

Quick links

Citations

17 review citations

Penicillin-binding proteins and beta-lactam resistance.
Zapun et al. (2008)
16 more

5 mentions without citation

Genetic analysis of the cell division protein FtsI (PBP3): amino acid substitutions that impair septal localization of FtsI and recruitment of FtsN.
Wissel et al. (2004)
4 more