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| | ==Structure of SusE with alpha-cyclodextrin== | | ==Structure of SusE with alpha-cyclodextrin== |
| - | <StructureSection load='4fem' size='340' side='right' caption='[[4fem]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='4fem' size='340' side='right'caption='[[4fem]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4fem]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bactn Bactn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FEM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FEM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4fem]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron_VPI-5482 Bacteroides thetaiotaomicron VPI-5482]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FEM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACX:ALPHA-CYCLODEXTRIN+(CYCLOHEXA-AMYLOSE)'>ACX</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | + | </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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900015:alpha-cyclodextrin'>PRD_900015</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fch|4fch]], [[4fe9|4fe9]]</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=4fem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fem OCA], [https://pdbe.org/4fem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fem RCSB], [https://www.ebi.ac.uk/pdbsum/4fem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fem ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BT_3700, susE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=226186 BACTN])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fem OCA], [http://pdbe.org/4fem PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fem RCSB], [http://www.ebi.ac.uk/pdbsum/4fem PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fem ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SUSE_BACTN SUSE_BACTN]] Starch-binding protein present at the surface of the cell. Mediates starch-binding before starch transport in the periplasm for degradation. SusE and SusF do not constitute the major starch-binding proteins in starch degradation pathway. Has higher affinity for starch compared to SusF.<ref>PMID:10986238</ref> <ref>PMID:11717282</ref> <ref>PMID:22910908</ref> | + | [https://www.uniprot.org/uniprot/SUSE_BACTN SUSE_BACTN] Starch-binding protein present at the surface of the cell. Mediates starch-binding before starch transport in the periplasm for degradation. SusE and SusF do not constitute the major starch-binding proteins in starch degradation pathway. Has higher affinity for starch compared to SusF.<ref>PMID:10986238</ref> <ref>PMID:11717282</ref> <ref>PMID:22910908</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bactn]] | + | [[Category: Bacteroides thetaiotaomicron VPI-5482]] |
| - | [[Category: Cameron, E A]] | + | [[Category: Large Structures]] |
| - | [[Category: Koropatkin, N M]] | + | [[Category: Cameron EA]] |
| - | [[Category: Martens, E C]] | + | [[Category: Koropatkin NM]] |
| - | [[Category: Carbohydrate-binding protein]] | + | [[Category: Martens EC]] |
| - | [[Category: Extracellular]]
| + | |
| - | [[Category: Outermembrane]]
| + | |
| - | [[Category: Starch binding]]
| + | |
| Structural highlights
Function
SUSE_BACTN Starch-binding protein present at the surface of the cell. Mediates starch-binding before starch transport in the periplasm for degradation. SusE and SusF do not constitute the major starch-binding proteins in starch degradation pathway. Has higher affinity for starch compared to SusF.[1] [2] [3]
Publication Abstract from PubMed
Human colonic bacteria are necessary for the digestion of many dietary polysaccharides. The intestinal symbiont Bacteroides thetaiotaomicron uses five outer membrane proteins to bind and degrade starch. Here, we report the x-ray crystallographic structures of SusE and SusF, two outer membrane proteins composed of tandem starch specific carbohydrate-binding modules (CBMs) with no enzymatic activity. Examination of the two CBMs in SusE and three CBMs in SusF reveals subtle differences in the way each binds starch and is reflected in their Kds for both high molecular weight starch and small maltooligosaccharides. Thus, each site seems to have a unique starch preference that may enable these proteins to interact with different regions of starch or its breakdown products. Proteins similar to SusE and SusF are encoded in many other polysaccharide utilization loci that are possessed by human gut bacteria in the phylum Bacteroidetes. Thus, these proteins are likely to play an important role in carbohydrate metabolism in these abundant symbiotic species. Understanding structural changes that diversify and adapt related proteins in the human gut microbial community will be critical to understanding the detailed mechanistic roles that they perform in the complex digestive ecosystem.
Multi-domain carbohydrate-binding proteins involved in Bacteroides thetaiotaomicron starch metabolism.,Cameron EA, Maynard MA, Smith CJ, Smith TJ, Koropatkin NM, Martens EC J Biol Chem. 2012 Aug 21. PMID:22910908[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shipman JA, Berleman JE, Salyers AA. Characterization of four outer membrane proteins involved in binding starch to the cell surface of Bacteroides thetaiotaomicron. J Bacteriol. 2000 Oct;182(19):5365-72. PMID:10986238
- ↑ Cho KH, Salyers AA. Biochemical analysis of interactions between outer membrane proteins that contribute to starch utilization by Bacteroides thetaiotaomicron. J Bacteriol. 2001 Dec;183(24):7224-30. PMID:11717282
- ↑ Cameron EA, Maynard MA, Smith CJ, Smith TJ, Koropatkin NM, Martens EC. Multi-domain carbohydrate-binding proteins involved in Bacteroides thetaiotaomicron starch metabolism. J Biol Chem. 2012 Aug 21. PMID:22910908 doi:http://dx.doi.org/10.1074/jbc.M112.397380
- ↑ Cameron EA, Maynard MA, Smith CJ, Smith TJ, Koropatkin NM, Martens EC. Multi-domain carbohydrate-binding proteins involved in Bacteroides thetaiotaomicron starch metabolism. J Biol Chem. 2012 Aug 21. PMID:22910908 doi:http://dx.doi.org/10.1074/jbc.M112.397380
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