› 3gmw

X-ray diffraction
2.1Å resolution

Crystal Structure of Beta-Lactamse Inhibitory Protein-I (BLIP-I) in Complex with TEM-1 Beta-Lactamase

Released:
DOI: 10.2210/pdb3gmw/pdb
PDB entry 3gmw coloured by chain, front view.
PDB entry 3gmw coloured by chain, side view.
PDB entry 3gmw coloured by chain, top view.
Source organisms:
Primary publication:
Insights into positive and negative requirements for protein-protein interactions by crystallographic analysis of the beta-lactamase inhibitory proteins BLIP, BLIP-I, and BLP.
Gretes M, Lim DC, de Castro L, Jensen SE, Kang SG, Lee KJ, Strynadka NC
J Mol Biol 389 289-305 (2009)
PMID: 19332077

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107714 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Beta-lactamase Chains: A, C
Molecule details ›
Chains: A, C
Length: 261 amino acids
Theoretical weight: 28.73 KDa
Source organism: Escherichia sp. Sflu5
Expression system: Escherichia coli
UniProt:
  • Canonical: A5PHA6 (Residues: 26-286; Coverage: 99%)
Gene name: amp
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily
Beta-lactamase inhibitory protein BLIP-I precusor Chains: B, D
Molecule details ›
Chains: B, D
Length: 156 amino acids
Theoretical weight: 17.22 KDa
Source organism: Streptomyces exfoliatus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9KJ90 (Residues: 31-186; Coverage: 99%)
Gene name: bliA
Sequence domains: Beta-lactamase inhibitor (BLIP)
Structure domains: BLIP domain

Ligands and Environments

1 bound ligand:
Ligand PO4 4 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P1
Unit cell:
a: 45.418Å b: 48.757Å c: 106.137Å
α: 103.24° β: 91.29° γ: 90.18°
R-values:
R R work R free
0.195 0.192 0.234
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Designing specific protein-protein interactions using computation, experimental library screening, or integrated methods.
Chen et al. (2012)
3 more

2 mentions without citation

Protein binding specificity versus promiscuity.
Schreiber et al. (2011)
1 more