8hui
From Proteopedia
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<table><tr><td colspan='2'>[[8hui]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_peucetius_subsp._caesius_ATCC_27952 Streptomyces peucetius subsp. caesius ATCC 27952]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HUI FirstGlance]. <br> | <table><tr><td colspan='2'>[[8hui]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_peucetius_subsp._caesius_ATCC_27952 Streptomyces peucetius subsp. caesius ATCC 27952]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HUI FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.44Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.44Å</td></tr> | ||
| - | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=Z9N: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=Z9N:(2S,3S,4S,5R)-2,5-bis(hydroxymethyl)oxolane-2,3,4-triol'>Z9N</scene></td></tr> |
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8hui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hui OCA], [https://pdbe.org/8hui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hui RCSB], [https://www.ebi.ac.uk/pdbsum/8hui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hui ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8hui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hui OCA], [https://pdbe.org/8hui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hui RCSB], [https://www.ebi.ac.uk/pdbsum/8hui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hui ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == | + | <div style="background-color:#fffaf0;"> |
| - | + | == Publication Abstract from PubMed == | |
| + | Carbohydrate degradation is crucial for living organisms due to their essential functions in providing energy and composing various metabolic pathways. Nevertheless, in the catalytic cycle of polysaccharide degradation, the details of how the substrates bind and how the products release need more case studies. Here, we choose an inulin fructotransferase (SpIFTase) as a model system, which can degrade inulin into functionally difructose anhydride I. At first, the crystal structures of SpIFTase in the absence of carbohydrates and complex with fructosyl-nystose (GF4), difructose anhydride I, and fructose are obtained, giving the substrate trajectory and product path of SpIFTase, which are further supported by steered molecular dynamics simulations (MDSs) along with mutagenesis. Furthermore, structural topology variations at the active centers of inulin fructotransferases are suggested as the structural base for product release, subsequently proven by substitution mutagenesis and MDSs. Therefore, this study provides a case in point for a deep understanding of the catalytic cycle with substrate trajectory and product path. | ||
| + | |||
| + | Structural Insights into the Catalytic Cycle of Inulin Fructotransferase: From Substrate Anchoring to Product Releasing.,Cheng M, Hou X, Huang Z, Chen Z, Ni D, Zhang W, Rao Y, Mu W J Agric Food Chem. 2024 Jul 31;72(30):17030-17040. doi: 10.1021/acs.jafc.4c03615. , Epub 2024 Jul 22. PMID:39034843<ref>PMID:39034843</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8hui" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of DFA I-forming Inulin Lyase from Streptomyces peucetius subsp. caesius ATCC 27952 in complex with GF4, DFA I, and fructose
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