› 2w22

X-ray diffraction
2.2Å resolution

Activation Mechanism of Bacterial Thermoalkalophilic Lipases

Released:
DOI: 10.2210/pdb2w22/pdb
PDB entry 2w22 coloured by chain, front view.
PDB entry 2w22 coloured by chain, side view.
PDB entry 2w22 coloured by chain, top view.
Source organism: Geobacillus thermocatenulatus
Primary publication:
Activation of bacterial thermoalkalophilic lipases is spurred by dramatic structural rearrangements.
Carrasco-López C, Godoy C, de Las Rivas B, Fernández-Lorente G, Palomo JM, Guisán JM, Fernández-Lafuente R, Martínez-Ripoll M, Hermoso JA
J Biol Chem 284 4365-72 (2009)
PMID: 19056729

Function and Biology Details

Reaction catalysed: 
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176785 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
triacylglycerol lipase Chain: A
Molecule details ›
Chain: A
Length: 389 amino acids
Theoretical weight: 43.37 KDa
Source organism: Geobacillus thermocatenulatus
Expression system: Escherichia coli DH5[alpha]
UniProt:
  • Canonical: Q59260 (Residues: 30-417; Coverage: 93%)
Structure domains: alpha/beta hydrolase

Ligands and Environments

4 bound ligands:
Ligand CA 1 x CA
Ligand ZN 1 x ZN
Ligand EGC 2 x EGC
Ligand MPD 3 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM16
Spacegroup: I222
Unit cell:
a: 73.07Å b: 128.08Å c: 127.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.182 0.226
Expression system: Escherichia coli DH5[alpha]

Quick links

Citations

10 review citations

Modifying enzyme activity and selectivity by immobilization.
Rodrigues et al. (2013)
9 more

20 mentions without citation

Microbial Lipases and Their Potential in the Production of Pharmaceutical Building Blocks.
Godoy et al. (2022)
19 more