This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1st8
From Proteopedia
|
Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus
Overview
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).
About this Structure
1ST8 is a Single protein structure of sequence from Cichorium intybus with GOL as ligand. Active as Fructan beta-fructosidase, with EC number 3.2.1.80 Full crystallographic information is available from OCA.
Reference
X-ray diffraction structure of a plant glycosyl hydrolase family 32 protein: fructan 1-exohydrolase IIa of Cichorium intybus., Verhaest M, Ende WV, Roy KL, De Ranter CJ, Laere AV, Rabijns A, Plant J. 2005 Feb;41(3):400-11. PMID:15659099
Page seeded by OCA on Sun Nov 25 01:06:37 2007
