› 3gmv

X-ray diffraction
1.8Å resolution

Crystal Structure of Beta-Lactamse Inhibitory Protein-I (BLIP-I) in Apo Form

Released:
DOI: 10.2210/pdb3gmv/pdb
PDB entry 3gmv coloured by chain, front view.
PDB entry 3gmv coloured by chain, side view.
PDB entry 3gmv coloured by chain, top view.
Source organism: Streptomyces exfoliatus
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

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191902 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase inhibitory protein BLIP-I precusor Chain: X
Molecule details ›
Chain: X
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 TAM 1 x TAM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: C2
Unit cell:
a: 98.735Å b: 44.071Å c: 45.291Å
α: 90° β: 104.58° γ: 90°
R-values:
R R work R free
0.187 0.185 0.227
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

2 mentions without citation

Structural basis of outer membrane protein biogenesis in bacteria.
Albrecht et al. (2011)
1 more