› 3m83

X-ray diffraction
2.12Å resolution

Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.12 A resolution (paraoxon inhibitor complex structure)

Released:
DOI: 10.2210/pdb3m83/pdb
PDB entry 3m83 coloured by chain, front view.
PDB entry 3m83 coloured by chain, side view.
PDB entry 3m83 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima.
Levisson M, Han GW, Deller MC, Xu Q, Biely P, Hendriks S, Ten Eyck LF, Flensburg C, Roversi P, Miller MD, McMullan D, von Delft F, Kreusch A, Deacon AM, van der Oost J, Lesley SA, Elsliger MA, Kengen SW, Wilson IA
Proteins 80 1545-59 (2012)
PMID: 22411095

Function and Biology Details

Reactions catalysed: 
Cephalosporin C + H(2)O = deacetylcephalosporin C + acetate
Deacetylation of xylans and xylo-oligosaccharides
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194439 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cephalosporin-C deacetylase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 337 amino acids
Theoretical weight: 38.8 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WXT2 (Residues: 1-325; Coverage: 100%)
Gene names: TM_0077, axeA
Sequence domains: Acetyl xylan esterase (AXE1)
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
Ligand CA 8 x CA
Ligand EDO 12 x EDO
Ligand ACT 3 x ACT
1 modified residue:
Ligand SDP 6 x SDP

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P212121
Unit cell:
a: 103.797Å b: 104.431Å c: 221.644Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.168 0.205
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Microbial carbohydrate esterases deacetylating plant polysaccharides.
Biely P. (2012)
4 more

4 mentions without citation

Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima.
Levisson et al. (2012)
3 more