3UW0

Pectin methylesterase from Yersinia enterocolitica

3UW0 の概要

• エントリーDOI: 10.2210/pdb3uw0/pdb
• 分子名称: pectinesterase (2 entities in total)
• 機能のキーワード: right-handed beta-helix, carbohydrate esterase, hydrolase
• 由来する生物種: Yersinia enterocolitica subsp. enterocolitica
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39784.46

構造登録者

Abbott, D.W.,Boraston, A.B. (登録日: 2011-11-30, 公開日: 2012-02-08, 最終更新日: 2023-09-13)

主引用文献

Boraston, A.B.,Abbott, D.W.
Structure of a pectin methylesterase from Yersinia enterocolitica.
Acta Crystallogr.,Sect.F, 68:129-133, 2012

PubMed Abstract: Pectin methylesterases (PMEs) are family 8 carbohydrate esterases (CE8s) which remove the methyl group from methylesterified galacturonic acid (GalA) residues within pectin. Although the role of pectinases such as PMEs within dedicated phytopathogens has been well established, the significance of homologous enzymes found within the genomes of human enteropathogens remains to be determined. Presented here is the low-resolution (3.5 Å) structure of the CE8 from Yersinia enterocolitica (YeCE8). The high degree of structural conservation in the topology of the active-site cleft and catalytic apparatus that is shared with a characterized PME from a bacterial phytopathogen (i) indicates that YeCE8 is active on methylated pectin and (ii) highlights a more prominent role for pectin utilization in Yersinia than in other enteropathogenic species.

PubMed: 22297983
DOI: 10.1107/S1744309111055400

実験手法

X-RAY DIFFRACTION (3.5 Å)