5xnr
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Truncated AlyQ with CBM32 and alginate lyase domains== | |
| + | <StructureSection load='5xnr' size='340' side='right' caption='[[5xnr]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5xnr]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XNR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XNR 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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5xnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xnr OCA], [http://pdbe.org/5xnr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xnr RCSB], [http://www.ebi.ac.uk/pdbsum/5xnr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xnr ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | AlyQ from Persicobacter sp. CCB-QB2 is an alginate lyase with three domains - a carbohydrate-binding domain modestly resembling family 16 carbohydrate-binding module (CBM16), a family 32 CBM (CBM32) domain, and an alginate lyase domain belonging to polysaccharide lyase family 7 (PL7). Although AlyQ can also act on polyguluronate (poly-G) and polymannuronate (poly-M), it is most active on alginate. Studies with truncated AlyQ showed that the CBM32 domain did not contribute to enhancing AlyQ's activity under the assayed conditions. Nevertheless, it could bind to cleaved but not intact alginate, indicating that the CBM32 domain recognises alginate termini. The crystal structure containing both CBM32 and catalytic domains show that they do not interact with one another. The CBM32 domain contains a conserved Arg that may bind to the carboxyl group of alginate. The catalytic domain, meanwhile, shares a conserved substrate-binding groove, and the presence of two negatively charged Asp residues may dictate substrate specificity especially at subsite +1. As Persicobacter sp. CCB-QB2 was unable to utilise alginate, AlyQ may function to help the bacterium degrade cell walls more efficiently. | ||
| - | + | Functional and Structural Studies of a Multidomain Alginate Lyase from Persicobacter sp. CCB-QB2.,Sim PF, Furusawa G, Teh AH Sci Rep. 2017 Oct 20;7(1):13656. doi: 10.1038/s41598-017-13288-1. PMID:29057942<ref>PMID:29057942</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Teh, A | + | <div class="pdbe-citations 5xnr" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Sim, P F]] | ||
| + | [[Category: Teh, A H]] | ||
| + | [[Category: Alginate lyase]] | ||
| + | [[Category: Cbm32]] | ||
| + | [[Category: Lyase]] | ||
Revision as of 07:34, 14 June 2018
Truncated AlyQ with CBM32 and alginate lyase domains
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Categories: Sim, P F | Teh, A H | Alginate lyase | Cbm32 | Lyase
