1JRG

Crystal Structure of the R3 form of Pectate Lyase A, Erwinia chrysanthemi

1JRG の概要

• エントリーDOI: 10.2210/pdb1jrg/pdb
• 関連するPDBエントリー: 1JTA
• 分子名称: Pectate lyase, SULFATE ION (3 entities in total)
• 機能のキーワード: parallel beta helix beta elimination, lyase
• 由来する生物種: Erwinia chrysanthemi
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77973.47

構造登録者

Thomas, L.M.,Doan, C.,Oliver, R.L.,Yoder, M.D. (登録日: 2001-08-13, 公開日: 2002-06-19, 最終更新日: 2024-11-06)

主引用文献

Thomas, L.M.,Doan, C.N.,Oliver, R.L.,Yoder, M.D.
Structure of pectate lyase A: comparison to other isoforms.
Acta Crystallogr.,Sect.D, 58:1008-1015, 2002

PubMed Abstract: Pectate lyase A is a virulence factor secreted by the plant-pathogenic bacteria Erwinia chrysanthemi. The enzyme cleaves the glycosidic bond of pectate polymers by a calcium-dependent beta-elimination mechanism. The crystal structure of pectate lyase A from E. chrysanthemi EC16 has been determined in two crystal forms, monoclinic C2 to 1.8 A and rhombohedral R3 to 2.1 A. The protein structure is compared with two other pectate lyase isoforms from E. chrysanthemi EC16, pectate lyase C and pectate lyase E. Pectate lyase A is unique as it is the only acidic pectate lyase and has end products that are significantly more varied in length in comparison to those of the other four major pectate lyase isozymes. Differences and similarities in polypeptide trace, size and volume of the active-site groove and surface electrostatics are discussed.

PubMed: 12037303
DOI: 10.1107/S0907444902005851

実験手法

X-RAY DIFFRACTION (2.1 Å)