› 4f21

X-ray diffraction
2.5Å resolution

Crystal structure of carboxylesterase/phospholipase family protein from Francisella tularensis

Released:
DOI: 10.2210/pdb4f21/pdb
PDB entry 4f21 coloured by chain, front view.
PDB entry 4f21 coloured by chain, side view.
PDB entry 4f21 coloured by chain, top view.
Source organism: Francisella tularensis subsp. tularensis SCHU S4
Primary publication:
Large scale structural rearrangement of a serine hydrolase from Francisella tularensis facilitates catalysis.
Filippova EV, Weston LA, Kuhn ML, Geissler B, Gehring AM, Armoush N, Adkins CT, Minasov G, Dubrovska I, Shuvalova L, Winsor JR, Lavis LD, Satchell KJ, Becker DP, Anderson WF, Johnson RJ
J Biol Chem 288 10522-35 (2013)
PMID: 23430251

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177710 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipase/carboxylesterase/thioesterase domain-containing protein Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 246 amino acids
Theoretical weight: 27.44 KDa
Source organism: Francisella tularensis subsp. tularensis SCHU S4
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5NI32 (Residues: 1-222; Coverage: 100%)
Gene name: FTT_0258
Sequence domains: Phospholipase/Carboxylesterase
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand 0S1 1 x 0S1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P1
Unit cell:
a: 50.997Å b: 64.416Å c: 139.039Å
α: 94.89° β: 90.12° γ: 89.96°
R-values:
R R work R free
0.204 0.199 0.258
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Bright building blocks for chemical biology.
Lavis et al. (2014)
2 more

6 mentions without citation

Molecular Mechanism for Isoform-Selective Inhibition of Acyl Protein Thioesterases 1 and 2 (APT1 and APT2).
Won et al. (2016)
5 more