2ls6

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Current revision (06:57, 1 May 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ls6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens_ATCC_13124 Clostridium perfringens ATCC 13124]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LS6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2ls6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens_ATCC_13124 Clostridium perfringens ATCC 13124]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LS6 FirstGlance]. <br>
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</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=2ls6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ls6 OCA], [https://pdbe.org/2ls6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ls6 RCSB], [https://www.ebi.ac.uk/pdbsum/2ls6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ls6 ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ls6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ls6 OCA], [https://pdbe.org/2ls6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ls6 RCSB], [https://www.ebi.ac.uk/pdbsum/2ls6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ls6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/A0A0H2YRL1_CLOP1 A0A0H2YRL1_CLOP1]
[https://www.uniprot.org/uniprot/A0A0H2YRL1_CLOP1 A0A0H2YRL1_CLOP1]
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Carbohydrate-binding modules (CBMs) are ancillary modules commonly associated with carbohydrate-active enzymes (CAZymes) that function to mediate the adherence of the parent enzyme to its carbohydrate substrates. CBM family 32 (CBM32) is one of the most diverse CBM families, whose members are commonly found in bacterial CAZymes that modify eukaryotic glycans. One such example is the putative mu-toxin, CpGH84A, of the family 84 glycoside hydrolases, which comprises an N-terminal putative beta-N-acetylglucosaminidase catalytic module and four tandem CBM32s. Here, we report a unique mode of galactose recognition by the first CBM32, CBM32-1 from CpGH84A. Solution NMR-based analyses of CpGH84A CBM32-1 indicate a divergent subset of residues, located in ordered loops at the apex of the CBM, conferring specificity for the galacto-configured sugars galactose, GalNAc, and LacNAc that differs from those of the canonical galactose-binding CBM32s. This study showcases the impressive variability in ligand binding by this CBM family and offers insight into the growing role of these modules in the interaction of CAZymes with eukaryotic glycans.
 
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An Unusual Mode of Galactose Recognition by a Family 32 Carbohydrate-Binding Module.,Grondin JM, Chitayat S, Ficko-Blean E, Houliston S, Arrowsmith CH, Boraston AB, Smith SP J Mol Biol. 2013 Dec 8. pii: S0022-2836(13)00744-4. doi:, 10.1016/j.jmb.2013.11.029. PMID:24326248<ref>PMID:24326248</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 2ls6" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Solution NMR Structure of a Non-canonical galactose-binding CBM32 from Clostridium perfringens

PDB ID 2ls6

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