1PLU

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

1PLU の概要

• エントリーDOI: 10.2210/pdb1plu/pdb
• 分子名称: PROTEIN (PECTATE LYASE C), LUTETIUM (III) ION (2 entities in total)
• 機能のキーワード: pectate cleavage, pectinolytic activity, trans-elimination, parallel beta-helix, lyase
• 由来する生物種: Erwinia chrysanthemi
• 細胞内の位置: Secreted: P11073
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37908.57

構造登録者

Yoder, M.D.,Jurnak, F.A. (登録日: 1999-06-04, 公開日: 1999-07-13, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)