6b15: Difference between revisions

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==Crystal structure of CBMbc (family CBM26) from Eubacterium rectale Amy13K==
==Crystal structure of CBMbc (family CBM26) from Eubacterium rectale Amy13K==
<StructureSection load='6b15' size='340' side='right' caption='[[6b15]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='6b15' size='340' side='right'caption='[[6b15]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6b15]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B15 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B15 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6b15]] is a 4 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=6B15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6B15 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 2.1&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6az5|6az5]]</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></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=6b15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b15 OCA], [http://pdbe.org/6b15 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b15 RCSB], [http://www.ebi.ac.uk/pdbsum/6b15 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b15 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=6b15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b15 OCA], [https://pdbe.org/6b15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6b15 RCSB], [https://www.ebi.ac.uk/pdbsum/6b15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6b15 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/D6DYI9_9FIRM D6DYI9_9FIRM]
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6b15" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cockburn, D W]]
[[Category: Large Structures]]
[[Category: Koropatkin, N M]]
[[Category: Cockburn DW]]
[[Category: Medina, K Perez]]
[[Category: Koropatkin NM]]
[[Category: Wawrzak, Z]]
[[Category: Perez Medina K]]
[[Category: Amylase]]
[[Category: Wawrzak Z]]
[[Category: Carbohydrate binding module]]
[[Category: Eubacterium rectale]]
[[Category: Gut microbiome]]
[[Category: Starch]]
[[Category: Sugar binding protein]]

Latest revision as of 14:19, 13 March 2024

Crystal structure of CBMbc (family CBM26) from Eubacterium rectale Amy13K

6b15, resolution 2.10Å

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