1PLU: Pectate Lyase C From Erwinia Chrysanthemi With 1 Lu+3 Ion In The Putative Calcium Binding Site

The crystal structure of pectate lyase C (EC from the enterobacterium Erwinia chrysanthemi (PelC) has been refined by molecular dynamics techniques to a resolution of 2.2 A to an R factor of 17.97%. The final model consists of 352 of the total 353 amino acids and 114 solvent molecules. The root-mean-square deviation from ideality is 0.009 A for bond lengths and 1.768[deg] for bond angles. The structure of PelC bound to the lanthanide ion lutetium, used as a calcium analog, has also been refined. Lutetium inhibits the enzymatic activity of the protein, and in the PelC-lutetium structure, the ion binds in the putative calcium-binding site. Five side-chain atoms form ligands to the lutetium ion. An analysis of the atomic-level model of the two protein structures reveals possible implications for the enzymatic mechanism of the enzyme.
PDB ID: 1PLUDownload
MMDB ID: 10896
PDB Deposition Date: 1999/6/4
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.2  Å
Source Organism:
Similar Structures:
Biological Unit for 1PLU: monomeric; determined by author
Molecular Components in 1PLU
Label Count Molecule
Protein (1 molecule)
Protein (Pectate Lyase C)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB