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1st8

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Current revision (08:35, 1 May 2024) (edit) (undo)
 
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<StructureSection load='1st8' size='340' side='right'caption='[[1st8]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
<StructureSection load='1st8' size='340' side='right'caption='[[1st8]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[1st8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cichorium_intybus Cichorium intybus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1ST8 FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
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<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>
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<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>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1st8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1st8 OCA], [https://pdbe.org/1st8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1st8 RCSB], [https://www.ebi.ac.uk/pdbsum/1st8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1st8 ProSAT]</span></td></tr>
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<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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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q93X60_CICIN Q93X60_CICIN]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1st8 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1st8 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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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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>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1st8" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cicin]]
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[[Category: Cichorium intybus]]
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[[Category: Fructan beta-fructosidase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ende, W Van den]]
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[[Category: De Ranter CJ]]
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[[Category: Laere, A Van]]
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[[Category: Rabijns A]]
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[[Category: Rabijns, A]]
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[[Category: Van Laere A]]
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[[Category: Ranter, C J.De]]
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[[Category: Van den Ende W]]
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[[Category: Verhaest, M]]
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[[Category: Verhaest M]]
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[[Category: Five fold beta propeller]]
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[[Category: Hydrolase]]
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Current revision

Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus

PDB ID 1st8

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