1BHE

POLYGALACTURONASE FROM ERWINIA CAROTOVORA SSP. CAROTOVORA

1BHE の概要

• エントリーDOI: 10.2210/pdb1bhe/pdb
• 分子名称: POLYGALACTURONASE (2 entities in total)
• 機能のキーワード: family 28 glycosyl hydrolase, hydrolyses polygalacturonic acid, glycosidase
• 由来する生物種: Pectobacterium carotovorum subsp. carotovorum
• 細胞内の位置: Secreted: P26509
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40135.22

構造登録者

Pickersgill, R.,Smith, D.,Worboys, K.,Jenkins, J. (登録日: 1998-06-05, 公開日: 1998-11-11, 最終更新日: 2024-11-06)

主引用文献

Pickersgill, R.,Smith, D.,Worboys, K.,Jenkins, J.
Crystal structure of polygalacturonase from Erwinia carotovora ssp. carotovora.
J.Biol.Chem., 273:24660-24664, 1998

PubMed Abstract: The crystal structure of the 40-kDa endo-polygalacturonase from Erwinia carotovora ssp. carotovora was solved by multiple isomorphous replacement and refined at 1.9 A to a conventional crystallographic R-factor of 0.198 and Rfree of 0.239. This is the first structure of a polygalacturonase and comprises a 10 turn right-handed parallel beta-helix domain with two loop regions forming a "tunnel like" substrate-binding cleft. Sequence conservation indicates that the active site of polygalacturonase is between these two loop regions, and comparison of the structure of polygalacturonase with that of rhamnogalacturonase A from Aspergillus aculeatus enables two conserved aspartates, presumed to be catalytic residues, to be identified. An adjacent histidine, in accord with biochemical results, is also seen. A similarity in overall electrostatic properties of the substrate-binding clefts of polygalacturonase and pectate lyase, which bind and cleave the same substrate, polygalacturonic acid, is also revealed.

PubMed: 9733763
DOI: 10.1074/jbc.273.38.24660

実験手法

X-RAY DIFFRACTION (1.9 Å)