7xz8: Difference between revisions

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-'''Unreleased structure'''
-The entry 7xz8 is ON HOLD  until Paper Publication
+==Mutant (K141A) of the N-terminal domain of fucoidan lyase FdlA==
+<StructureSection load='7xz8' size='340' side='right'caption='[[7xz8]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7xz8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Flavobacteriaceae_bacterium_SA-0082 Flavobacteriaceae bacterium SA-0082]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XZ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XZ8 FirstGlance]. <br>
+</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=7xz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xz8 OCA], [https://pdbe.org/7xz8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xz8 RCSB], [https://www.ebi.ac.uk/pdbsum/7xz8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xz8 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Fucoidans represent a type of polyanionic fucose-containing sulfated polysaccharides (FCSPs) that are cleaved by fucoidan-degrading enzymes, producing low-molecular-weight fucoidans with multiple biological activities suitable for pharmacological use. Most of the reported fucoidan-degrading enzymes are glycoside hydrolases, which have been well studied for their structures and catalytic mechanisms. Little is known, however, about the rarer fucoidan lyases, primarily due to the lack of structural information. FdlA from Flavobacterium sp. SA-0082 is an endo-type fucoidan-degrading enzyme that cleaves the sulfated fuco-glucuronomannan (SFGM) through a lytic mechanism. Here, we report nine crystal structures of the catalytic N-terminal domain of FdlA (FdlA-NTD), in both its wild type (WT) and mutant forms, at resolutions ranging from 1.30 to 2.25 A. We show that the FdlA-NTD adopts a right-handed parallel beta-helix fold, and possesses a substrate binding site composed of a long groove and a unique alkaline pocket. Our structural, biochemical, and enzymological analyses strongly suggest that FdlA-NTD utilizes catalytic residues different from other beta-helix polysaccharide lyases, potentially representing a novel polysaccharide lyase family.
-Authors: Wang, J., Li, M., Pan, X.
+Structural and Biochemical Analysis Reveals Catalytic Mechanism of Fucoidan Lyase from Flavobacterium sp. SA-0082.,Wang J, Liu Z, Pan X, Wang N, Li L, Du Y, Li J, Li M Mar Drugs. 2022 Aug 20;20(8). pii: md20080533. doi: 10.3390/md20080533. PMID:36005536<ref>PMID:36005536</ref>
-Description: Mutant (K141A) of the N-terminal domain of fucoidan lyase FdlA
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Pan, X]]
+<div class="pdbe-citations 7xz8" style="background-color:#fffaf0;"></div>
-[[Category: Li, M]]
+== References ==
-[[Category: Wang, J]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Flavobacteriaceae bacterium SA-0082]]
+[[Category: Large Structures]]
+[[Category: Li M]]
+[[Category: Pan X]]
+[[Category: Wang J]]