1ST8

Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus

Summary for 1ST8

• Entry DOI: 10.2210/pdb1st8/pdb
• Descriptor: fructan 1-exohydrolase IIa, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: five fold beta propeller, hydrolase
• Biological source: Cichorium intybus (chicory)
• Total number of polymer chains: 1
• Total formula weight: 62495.28

Authors

Verhaest, M.,Van den Ende, W.,De Ranter, C.J.,Van Laere, A.,Rabijns, A. (deposition date: 2004-03-25, release date: 2005-03-01, Last modification date: 2024-10-30)

Primary citation

Verhaest, M.,van den Ende, W.,Roy, K.L.,De Ranter, C.J.,van Laere, A.,Rabijns, A.
X-ray diffraction structure of a plant glycosyl hydrolase family 32 protein: fructan 1-exohydrolase IIa of Cichorium intybus.
Plant J., 41:400-411, 2005

PubMed 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).

PubMed: 15659099
DOI: 10.1111/j.1365-313X.2004.02304.x

Experimental method

X-RAY DIFFRACTION (2.35 Å)