Back to Search Start Over

X-ray diffraction structure of a plant glycosyl hydrolase family 32 protein: fructan 1-exohydrolase IIa of Cichorium intybus

Authors :
Maureen, Verhaest
Wim, Van den Ende
Katrien Le, Roy
Camiel J, De Ranter
André Van, Laere
Anja, Rabijns
Source :
The Plant journal : for cell and molecular biology. 41(3)
Publication Year :
2005

Abstract

Fructan 1-exohydrolase, an enzyme involved in fructan degradation, belongs to the glycosyl hydrolase family 32. The structure of isoenzyme 1-FEH IIa from Cichorium intybus is described at a resolution of 2.35 A. The structure consists of an N-terminal fivefold beta-propeller domain connected to two C-terminal beta-sheets. The putative active site is located entirely in the beta-propeller domain and is formed by amino acids which are highly conserved within glycosyl hydrolase family 32. The fructan-binding site is thought to be in the cleft formed between the two domains. The 1-FEH IIa structure is compared with the structures of two homologous but functionally different enzymes: a levansucrase from Bacillus subtilis (glycosyl hydrolase family 68) and an invertase from Thermotoga maritima (glycosyl hydrolase family 32).

Details

ISSN :
09607412
Volume :
41
Issue :
3
Database :
OpenAIRE
Journal :
The Plant journal : for cell and molecular biology
Accession number :
edsair.pmid..........1ee627280d601002b011a8073712a8d9