6az5: Difference between revisions
New page: '''Unreleased structure''' The entry 6az5 is ON HOLD Authors: Cockburn, D.W., Wawrzak, Z., Suh, C., Koropatkin, N.M. Description: Crystal structure of CBMd (family CBM41) from Eubacter... |
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The | ==Crystal structure of CBMd (family CBM41) from Eubacterium rectale Amy13K== | ||
<StructureSection load='6az5' size='340' side='right'caption='[[6az5]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6az5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Eubacterium_rectale_DSM_17629 Eubacterium rectale DSM 17629]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AZ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AZ5 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]] 2.2Å</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=6az5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6az5 OCA], [https://pdbe.org/6az5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6az5 RCSB], [https://www.ebi.ac.uk/pdbsum/6az5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6az5 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/D6DYI9_9FIRM D6DYI9_9FIRM] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Gut bacteria recognize accessible glycan substrates within a complex environment. Carbohydrate binding modules (CBMs) of cell-surface glycoside hydrolases often drive binding to the target substrate. Eubacterium rectale, an important butyrate-producing organism in the gut, consumes a limited range of substrates, including starch. Host consumption of resistant starch increases the abundance of E. rectale in the intestine, likely because it successfully captures the products of resistant starch degradation by other bacteria. Here we demonstrate that the cell wall anchored starch-degrading alpha-amylase, Amy13K of E. rectale harbors five CBMs that all target starch with differing specificities. Intriguingly these CBMs efficiently bind to both regular and high amylose corn starch (a type of resistant starch), but have almost no affinity for potato starch (another type of resistant starch). Removal of these CBMs from Amy13K reduces the activity level of the enzyme towards corn starches by approximately 40-fold, down to the level of activity towards potato starch, suggesting that the CBMs facilitate activity on corn starch and allowing its utilization in vivo. The specificity of the Amy13K CBMs provides a molecular rationale for why E. rectale is able to only use certain starch types without the aid of other organisms. | |||
Novel carbohydrate binding modules in the surface anchored alpha-amylase of Eubacterium rectale provide a molecular rationale for the range of starches used by this organism in the human gut.,Cockburn DW, Suh C, Medina KP, Duvall RM, Wawrzak Z, Henrissat B, Koropatkin NM Mol Microbiol. 2017 Nov 15. doi: 10.1111/mmi.13881. PMID:29139580<ref>PMID:29139580</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6az5" style="background-color:#fffaf0;"></div> | ||
[[Category: Koropatkin | |||
[[Category: Suh | ==See Also== | ||
[[Category: | *[[Amylase 3D structures|Amylase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Cockburn DW]] | |||
[[Category: Koropatkin NM]] | |||
[[Category: Suh C]] | |||
[[Category: Wawrzak Z]] | |||
Latest revision as of 13:06, 22 May 2024
Crystal structure of CBMd (family CBM41) from Eubacterium rectale Amy13KCrystal structure of CBMd (family CBM41) from Eubacterium rectale Amy13K
Structural highlights
FunctionPublication Abstract from PubMedGut bacteria recognize accessible glycan substrates within a complex environment. Carbohydrate binding modules (CBMs) of cell-surface glycoside hydrolases often drive binding to the target substrate. Eubacterium rectale, an important butyrate-producing organism in the gut, consumes a limited range of substrates, including starch. Host consumption of resistant starch increases the abundance of E. rectale in the intestine, likely because it successfully captures the products of resistant starch degradation by other bacteria. Here we demonstrate that the cell wall anchored starch-degrading alpha-amylase, Amy13K of E. rectale harbors five CBMs that all target starch with differing specificities. Intriguingly these CBMs efficiently bind to both regular and high amylose corn starch (a type of resistant starch), but have almost no affinity for potato starch (another type of resistant starch). Removal of these CBMs from Amy13K reduces the activity level of the enzyme towards corn starches by approximately 40-fold, down to the level of activity towards potato starch, suggesting that the CBMs facilitate activity on corn starch and allowing its utilization in vivo. The specificity of the Amy13K CBMs provides a molecular rationale for why E. rectale is able to only use certain starch types without the aid of other organisms. Novel carbohydrate binding modules in the surface anchored alpha-amylase of Eubacterium rectale provide a molecular rationale for the range of starches used by this organism in the human gut.,Cockburn DW, Suh C, Medina KP, Duvall RM, Wawrzak Z, Henrissat B, Koropatkin NM Mol Microbiol. 2017 Nov 15. doi: 10.1111/mmi.13881. PMID:29139580[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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