› 1o8m

X-ray diffraction
2.2Å resolution

Pectate Lyase C from Erwinia Chrysanthemi at pH 4.5 with no Ca2+ Added

Released:
DOI: 10.2210/pdb1o8m/pdb
PDB entry 1o8m coloured by chain, front view.
PDB entry 1o8m coloured by chain, side view.
PDB entry 1o8m coloured by chain, top view.
Source organism: Dickeya chrysanthemi
Primary publication:
Characterization and implications of Ca2+ binding to pectate lyase C.
Herron SR, Scavetta RD, Garrett M, Legner M, Jurnak F
J Biol Chem 278 12271-7 (2003)
PMID: 12540845

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:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145646 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pectate lyase C Chain: A
Molecule details ›
Chain: A
Length: 353 amino acids
Theoretical weight: 37.73 KDa
Source organism: Dickeya chrysanthemi
Expression system: Escherichia coli
UniProt:
  • Canonical: P11073 (Residues: 23-375; Coverage: 100%)
Gene name: pelC
Sequence domains: Pectate lyase
Structure domains: Single-stranded right-handed beta-helix, Pectin lyase-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RT3000
Spacegroup: P212121
Unit cell:
a: 72.94Å b: 80.75Å c: 95.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 0.215
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Structural and mechanistic classification of uronic acid-containing polysaccharide lyases.
Garron et al. (2010)
1 more

2 mentions without citation

Structural biology of pectin degradation by Enterobacteriaceae.
Abbott et al. (2008)
1 more