1st8

<table><tr><td colspan='2'>[[1st8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cicin Cicin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ST8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1ST8 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">1-feh IIa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13427 CICIN])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructan_beta-fructosidase Fructan beta-fructosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.80 3.2.1.80] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1st8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1st8 OCA], [http://pdbe.org/1st8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1st8 RCSB], [http://www.ebi.ac.uk/pdbsum/1st8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1st8 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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).

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<ref>PMID:15659099</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1st8" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Cicin]]

[[Category: Fructan beta-fructosidase]]

[[Category: Ende, W Van den]]

[[Category: Laere, A Van]]

[[Category: Rabijns, A]]

[[Category: Ranter, C J.De]]

[[Category: Verhaest, M]]

[[Category: Hydrolase]]