1CUS

FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME WITH A CATALYTIC SERINE ACCESSIBLE TO SOLVENT

1CUS の概要

• エントリーDOI: 10.2210/pdb1cus/pdb
• 分子名称: CUTINASE (2 entities in total)
• 機能のキーワード: hydrolase(serine esterase)
• 由来する生物種: Nectria haematococca mpVI
• 細胞内の位置: Secreted: P00590
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20742.28

構造登録者

Martinez, C.,Cambillau, C. (登録日: 1994-04-06, 公開日: 1994-07-31, 最終更新日: 2024-10-30)

主引用文献

Martinez, C.,De Geus, P.,Lauwereys, M.,Matthyssens, G.,Cambillau, C.
Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent.
Nature, 356:615-618, 1992

PubMed Abstract: Lipases belong to a class of esterases whose activity on triglycerides is greatly enhanced at lipid-water interfaces. This phenomenon, called interfacial activation, has a structural explanation: a hydrophobic lid, which at rest covers the catalytic site, is displaced on substrate or inhibitor binding and probably interacts with the lipid matrix. Fusarium solani pisi cutinase belongs to a group of homologous enzymes of relative molecular mass 22-25K (ref. 7) capable of degrading cutin, the insoluble lipid-polyester matrix covering the surface of plants, and hydrolysing triglycerides. Cutinases differ from classical lipases in that they do not exhibit interfacial activation; they are active on soluble as well as on emulsified triglycerides. Cutinases therefore establish a bridge between esterases and lipases. We report here the three-dimensional structure of a recombinant cutinase from F. solani pisi, expressed in Escherichia coli. Cutinase is an alpha-beta protein; the active site is composed of the triad Ser 120, His 188 and Asp 175. Unlike other lipases, the catalytic serine is not buried under surface loops, but is accessible to solvent. This could explain why cutinase does not display interfacial activation.

PubMed: 1560844
DOI: 10.1038/356615a0

実験手法

X-RAY DIFFRACTION (1.25 Å)