1OOC

Mutations in the T1.5 loop of pectate lyase A

1OOC の概要

• エントリーDOI: 10.2210/pdb1ooc/pdb
• 関連するPDBエントリー: 1JRG 1JTA
• 分子名称: Pectate lyase A (1 entity in total)
• 機能のキーワード: parallel beta helix, 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: 77479.07

構造登録者

Dehdashti, S.J.,Doan, C.N.,Chao, K.,Vordtriede, P.B.,Yoder, M.D. (登録日: 2003-03-03, 公開日: 2004-03-16, 最終更新日: 2024-10-16)

主引用文献

Dehdashti, S.J.,Doan, C.N.,Chao, K.L.,Yoder, M.D.
Effect of mutations in the T1.5 loop of pectate lyase A from Erwinia chrysanthemi EC16.
Acta Crystallogr.,Sect.D, 59:1339-1342, 2003

PubMed Abstract: Pectate lyase A (PelA) is a pectate-degrading enzyme secreted by plant pathogens. PelA from Erwinia chrysanthemi has 61% amino-acid identity and a conserved structural similarity to pectate lyase E (PelE). Although similar in structure and sequence, the enzymatic characteristics of PelA differ from those for PelE. A structural alignment of PelA and PelE reveals differences in the T1.5 loop. The sequence of the T1.5 loop in PelA was mutated to the homologous sequence in PelE. The crystal structure of the PelA T1.5 mutant has been solved to 1.6 and 2.9 A resolution. The enzymatic and structural properties of the T1.5 mutant are discussed.

PubMed: 12832805
DOI: 10.1107/S0907444903011491

実験手法

X-RAY DIFFRACTION (2.94 Å)