› 3b90

X-ray diffraction
2.11Å resolution

Crystal Structure of the Catalytic Domain of Pectate Lyase PelI from Erwinia chrysanthemi

Released:
DOI: 10.2210/pdb3b90/pdb
Model geometry
Fit model/data
PDB entry 3b90 coloured by chain, front view.
PDB entry 3b90 coloured by chain, side view.
PDB entry 3b90 coloured by chain, top view.
Source organism: Dickeya chrysanthemi
Primary publication:
The crystal structure of pectate lyase peli from soft rot pathogen Erwinia chrysanthemi in complex with its substrate.
Creze C, Castang S, Derivery E, Haser R, Hugouvieux-Cotte-Pattat N, Shevchik VE, Gouet P
J Biol Chem 283 18260-8 (2008)
PMID: 18430740

Function and Biology Details

Reaction catalysed: 
Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-129315 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pectate lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 226 amino acids
Theoretical weight: 23.85 KDa
Source organism: Dickeya chrysanthemi
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O50325 (Residues: 119-344; Coverage: 70%)
Gene name: pelI
Sequence domains: Pectate lyase
Structure domains: Single-stranded right-handed beta-helix, Pectin lyase-like

Ligands and Environments

3 bound ligands:
Ligand CA 2 x CA
Ligand ZN 4 x ZN
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P212121
Unit cell:
a: 45.4Å b: 62.6Å c: 128.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.21 0.273
Expression system: Escherichia coli BL21(DE3)

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Citations

5 review citations

The type II secretion system: biogenesis, molecular architecture and mechanism.
Korotkov et al. (2012)
4 more

3 mentions without citation

Evolution and functional characterization of pectate lyase PEL12, a member of a highly expanded Clonostachys rosea polysaccharide lyase 1 family.
Atanasova et al. (2018)
2 more