1st8

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{{STRUCTURE_1st8| PDB=1st8 | SCENE= }}
{{STRUCTURE_1st8| PDB=1st8 | SCENE= }}
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'''Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus'''
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===Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus===
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==Overview==
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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).
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(as it appears on PubMed at http://www.pubmed.gov), where 15659099 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15659099}}
==About this Structure==
==About this Structure==
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[[Category: Verhaest, M.]]
[[Category: Verhaest, M.]]
[[Category: Five fold beta propeller]]
[[Category: Five fold beta propeller]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:37:35 2008''

Revision as of 21:37, 27 July 2008

Image:1st8.png

Template:STRUCTURE 1st8

Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus

Template:ABSTRACT PUBMED 15659099

About this Structure

1ST8 is a Single protein structure of sequence from Cichorium intybus. 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

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