› 4c2l

X-ray diffraction
1.75Å resolution

Crystal structure of endo-xylogalacturonan hydrolase from Aspergillus tubingensis

Released:
DOI: 10.2210/pdb4c2l/pdb
PDB entry 4c2l coloured by chain, front view.
PDB entry 4c2l coloured by chain, side view.
PDB entry 4c2l coloured by chain, top view.
Source organism: Aspergillus tubingensis
Primary publication:
Crystal structure of endo-xylogalacturonan hydrolase from Aspergillus tubingensis.
Rozeboom HJ, Beldman G, Schols HA, Dijkstra BW
FEBS J 280 6061-9 (2013)
PMID: 24034788

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-194107 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Endo-xylogalacturonan hydrolase A Chain: A
Molecule details ›
Chain: A
Length: 388 amino acids
Theoretical weight: 40.16 KDa
Source organism: Aspergillus tubingensis
Expression system: Aspergillus niger
UniProt:
  • Canonical: Q9UUZ2 (Residues: 19-406; Coverage: 100%)
Gene name: xghA
Sequence domains: Glycosyl hydrolases family 28
Structure domains: Single-stranded right-handed beta-helix, Pectin lyase-like

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
4 bound ligands:
Ligand MAN 1 x MAN
Ligand NAG 1 x NAG
Ligand SO4 7 x SO4
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: I222
Unit cell:
a: 76.44Å b: 121.18Å c: 129.67Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.167 0.189
Expression system: Aspergillus niger

Quick links

Citations

2 citation in other articles

Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules.
Paxman et al. (2019)
1 more

5 mentions without citation

Molecular evidence for the involvement of a polygalacturonase-inhibiting protein, GhPGIP1, in enhanced resistance to Verticillium and Fusarium wilts in cotton.
Liu et al. (2017)
4 more