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| | ==SusG with mixed linkage amylosaccharide== | | ==SusG with mixed linkage amylosaccharide== |
| - | <StructureSection load='6bs6' size='340' side='right' caption='[[6bs6]], [[Resolution|resolution]] 2.17Å' scene=''> | + | <StructureSection load='6bs6' size='340' side='right'caption='[[6bs6]], [[Resolution|resolution]] 2.17Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6bs6]] is a 2 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=6BS6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BS6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6bs6]] is a 2 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=6BS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BS6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 2.17Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">susG, BT_3698 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=226186 BACTN])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRD_900009:alpha-maltotriose'>PRD_900009</scene>, <scene name='pdbligand=PRD_900010:alpha-maltotetraose'>PRD_900010</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] </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=6bs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bs6 OCA], [https://pdbe.org/6bs6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bs6 RCSB], [https://www.ebi.ac.uk/pdbsum/6bs6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bs6 ProSAT]</span></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=6bs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bs6 OCA], [http://pdbe.org/6bs6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bs6 RCSB], [http://www.ebi.ac.uk/pdbsum/6bs6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bs6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SUSG_BACTN SUSG_BACTN]] Alpha-amylase that cleaves starch into oligosaccharides before internalization for degradation, the first step in starch degradation.<ref>PMID:10572122</ref> <ref>PMID:11717282</ref> <ref>PMID:20159465</ref> | + | [https://www.uniprot.org/uniprot/SUSG_BACTN SUSG_BACTN] Alpha-amylase that cleaves starch into oligosaccharides before internalization for degradation, the first step in starch degradation.<ref>PMID:10572122</ref> <ref>PMID:11717282</ref> <ref>PMID:20159465</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Amylase|Amylase]] | + | *[[Amylase 3D structures|Amylase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alpha-amylase]] | + | [[Category: Bacteroides thetaiotaomicron VPI-5482]] |
| - | [[Category: Bactn]] | + | [[Category: Large Structures]] |
| - | [[Category: Cockburn, D W]] | + | [[Category: Cockburn DW]] |
| - | [[Category: Koropatkin, N M]] | + | [[Category: Koropatkin NM]] |
| - | [[Category: Amylase]]
| + | |
| - | [[Category: Gh13]]
| + | |
| - | [[Category: Glycoside hydrolase family 13]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Susg]]
| + | |
| Structural highlights
6bs6 is a 2 chain structure with sequence from Bacteroides thetaiotaomicron VPI-5482. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.17Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
SUSG_BACTN Alpha-amylase that cleaves starch into oligosaccharides before internalization for degradation, the first step in starch degradation.[1] [2] [3]
Publication Abstract from PubMed
Bacteria that reside in the mammalian intestinal tract efficiently hydrolyze dietary carbohydrates, including starch, that escape digestion in the small intestine. Starch is an abundant dietary carbohydrate comprised of alpha1,4 and alpha1,6 linked glucose, yet mammalian intestinal glucoamylases cannot effectively hydrolyze starch that has frequent alpha1,6 branching as these structures hinder recognition and processing by alpha1,4-specific amylases. Here we present the structure of the cell surface amylase SusG from Bacteroides thetaiotaomicron complexed with a mixed linkage amylosaccharide generated from transglycosylation during crystallization. Although SusG is specific for alpha1,4 glucosidic bonds, binding of this new oligosaccharide at the active site demonstrates that SusG can accommodate alpha1,6 branch points at subsite -3 to -2, and also at subsite+1 adjacent to the site of hydrolysis, explaining how this enzyme may be able to process a wide range of limit dextrins in the intestinal environment. These data suggest that B. thetaiotaomicron and related organisms may have a selective advantage for amylosaccharide scavenging in the gut.
Structural basis for the flexible recognition of alpha-glucan substrates by Bacteroides thetaiotaomicron SusG.,Arnal G, Cockburn DW, Brumer H, Koropatkin NM Protein Sci. 2018 Mar 30. doi: 10.1002/pro.3410. PMID:29603462[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shipman JA, Cho KH, Siegel HA, Salyers AA. Physiological characterization of SusG, an outer membrane protein essential for starch utilization by Bacteroides thetaiotaomicron. J Bacteriol. 1999 Dec;181(23):7206-11. PMID:10572122
- ↑ 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
- ↑ Koropatkin NM, Smith TJ. SusG: a unique cell-membrane-associated alpha-amylase from a prominent human gut symbiont targets complex starch molecules. Structure. 2010 Feb 10;18(2):200-15. PMID:20159465 doi:10.1016/j.str.2009.12.010
- ↑ Arnal G, Cockburn DW, Brumer H, Koropatkin NM. Structural basis for the flexible recognition of alpha-glucan substrates by Bacteroides thetaiotaomicron SusG. Protein Sci. 2018 Mar 30. doi: 10.1002/pro.3410. PMID:29603462 doi:http://dx.doi.org/10.1002/pro.3410
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