View source for 8xfq


==Structure of the alginate epimerase/lyase complexed with penta-mannuronic acid==
<StructureSection load='8xfq' size='340' side='right'caption='[[8xfq]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8xfq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_chroococcum_NCIMB_8003 Azotobacter chroococcum NCIMB 8003]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XFQ 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]] 2.25&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEM:BETA-D-MANNURONIC+ACID'>BEM</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=8xfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xfq OCA], [https://pdbe.org/8xfq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xfq RCSB], [https://www.ebi.ac.uk/pdbsum/8xfq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xfq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0C4WKK2_9GAMM A0A0C4WKK2_9GAMM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Among the epimerases specific to alginate, some of them in Azotobacter genera convert beta-d-mannuronic acid to alpha-l-guluronic acid but also have lyase activity to degrade alginate. The remarkable characteristics of these epimerases make it a promising enzyme for tailoring alginates to meet specific demands. Here, we determined the structure of the bifunctional mannuronan C-5 epimerase AlgE3 from Azotobacter chroococcum (AcAlgE3) in complex with several mannuronic acid oligomers as well as in apo form, which allowed us to elucidate the binding manner of each mannuronic acid oligomer, and the structural plasticity, which is dependent on calcium ions. Moreover, a comprehensive analysis of the lyase activity profiles of AcAlgE3 combined with structural characteristics explained the preference for different chain length oligomers.

Structural basis for the minimal bifunctional alginate epimerase AlgE3 from Azotobacter chroococcum.,Fujiwara T, Mano E, Nango E FEBS Lett. 2024 Apr 22. doi: 10.1002/1873-3468.14886. PMID:38649293<ref>PMID:38649293</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8xfq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Azotobacter chroococcum NCIMB 8003]]
[[Category: Large Structures]]
[[Category: Fujiwara T]]