7d29
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==CBM32 of AlyQ== | |
| + | <StructureSection load='7d29' size='340' side='right'caption='[[7d29]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7d29]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Persicobacter_sp._CCB-QB2 Persicobacter sp. CCB-QB2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D29 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]] 1.7Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=7d29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d29 OCA], [https://pdbe.org/7d29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d29 RCSB], [https://www.ebi.ac.uk/pdbsum/7d29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d29 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A3B6UEP6_9BACT A0A3B6UEP6_9BACT] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The alginate lyase AlyQ from Persicobacter sp. CCB-QB2 is a three-domained enzyme with a carbohydrate-binding module (CBM) from family 32. The CBM32 domain, AlyQB, binds enzymatically cleaved but not intact alginate. Co-crystallisation of AlyQB with the cleaved alginate reveals that it binds to the 4,5-unsaturated mannuronic acid of the non-reducing end. The binding pocket contains a conserved R248 that interacts with the sugar's carboxyl group, as well as an invariant W303 that stacks against the unsaturated pyranose ring. Targeting specifically the non-reducing end is more efficient than the reducing end since the latter consists of a mixture of mannuronic acid and guluronic acid. AlyQB also seems unable to bind these two saturated sugars as they contain OH groups that will clash with the pocket. Docking analysis of YeCBM32, which binds oligogalacturonic acid, shows that the stacking of the pyranose ring is shifted in order to accommodate the sugar's axial C1-OH, and its R69 is accordingly elevated to bind the sugar's carboxyl group. Unlike AlyQB, YeCBM32's binding pocket is able to accommodate both saturated and unsaturated galacturonic acid. | ||
| - | + | Structural basis for binding uronic acids by family 32 carbohydrate-binding modules.,Teh AH, Sim PF, Hisano T Biochem Biophys Res Commun. 2020 Dec 10;533(3):257-261. doi:, 10.1016/j.bbrc.2020.09.064. Epub 2020 Oct 1. PMID:33010888<ref>PMID:33010888</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7d29" style="background-color:#fffaf0;"></div> |
| - | [[Category: Sim | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Persicobacter sp. CCB-QB2]] | ||
| + | [[Category: Sim PF]] | ||
| + | [[Category: Teh AH]] | ||
Current revision
CBM32 of AlyQ
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