› 1plu

X-ray diffraction
2.2Å resolution

PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI WITH 1 LU+3 ION IN THE PUTATIVE CALCIUM BINDING SITE

Released:
DOI: 10.2210/pdb1plu/pdb
PDB entry 1plu coloured by chain, front view.
PDB entry 1plu coloured by chain, side view.
PDB entry 1plu coloured by chain, top view.
Source organism: Dickeya chrysanthemi
Primary publication:
The Refined Three-Dimensional Structure of Pectate Lyase C from Erwinia chrysanthemi at 2.2 Angstrom Resolution (Implications for an Enzymatic Mechanism).
Yoder MD, Jurnak F
Plant Physiol 107 349-364 (1995)
PMID: 12228363

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
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

1 bound ligand:
Ligand LU 1 x LU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 72.6Å b: 80.6Å c: 95.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.221 not available

Quick links

Citations

2 review citations

Homogalacturonan-modifying enzymes: structure, expression, and roles in plants.
Sénéchal et al. (2014)
1 more

2 mentions without citation

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