1PLU

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

Summary for 1PLU

• Entry DOI: 10.2210/pdb1plu/pdb
• Descriptor: PROTEIN (PECTATE LYASE C), LUTETIUM (III) ION (2 entities in total)
• Functional Keywords: pectate cleavage, pectinolytic activity, trans-elimination, parallel beta-helix, lyase
• Biological source: Erwinia chrysanthemi
• Cellular location: Secreted: P11073
• Total number of polymer chains: 1
• Total formula weight: 37908.57

Authors

Yoder, M.D.,Jurnak, F.A. (deposition date: 1999-06-04, release date: 1999-07-13, Last modification date: 2024-11-20)

Primary citation

Yoder, M.D.,Jurnak, F.
The Refined Three-Dimensional Structure of Pectate Lyase C from Erwinia chrysanthemi at 2.2 Angstrom Resolution (Implications for an Enzymatic Mechanism).
Plant Physiol., 107:349-364, 1995

PubMed Abstract: The crystal structure of pectate lyase C (EC 4.2.2.2) 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.

PubMed: 12228363

Experimental method

X-RAY DIFFRACTION (2.2 Å)