5lfz

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'''Unreleased structure'''
 
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The entry 5lfz is ON HOLD
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==T48 deacetylase==
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<StructureSection load='5lfz' size='340' side='right'caption='[[5lfz]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5lfz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrobacter_sp._AW19M34-1 Arthrobacter sp. AW19M34-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LFZ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.561&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></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=5lfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lfz OCA], [https://pdbe.org/5lfz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lfz RCSB], [https://www.ebi.ac.uk/pdbsum/5lfz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lfz ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Chitin, a polymer of beta(1-4)-linked N-acetylglucosamine found in e.g. arthropods, is a valuable resource that may be used to produce chitosan and chitooligosaccharides, two compounds with considerable industrial and biomedical potential. Deacetylating enzymes may be used to tailor the properties of chitin and its derived products. Here, we describe a novel CE4 enzyme originating from a marine Arthrobacter species (ArCE4A). Crystal structures of this novel deacetylase were determined, with and without bound chitobiose [(GlcNAc)2], and refined to 2.1 A and 1.6 A, respectively. In-depth biochemical characterization showed that ArCE4A has broad substrate specificity, with higher activity against longer oligosaccharides. Mass spectrometry-based sequencing of reaction products generated from a fully acetylated pentamer showed that internal sugars are more prone to deacetylation than the ends. These enzyme properties are discussed in the light of the structure of the enzyme-ligand complex, which adds valuable information to our still rather limited knowledge on enzyme-substrate interactions in the CE4 family.
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Authors: Rothweiler, U.
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Structure and function of a CE4 deacetylase isolated from a marine environment.,Tuveng TR, Rothweiler U, Udatha G, Vaaje-Kolstad G, Smalas A, Eijsink VGH PLoS One. 2017 Nov 6;12(11):e0187544. doi: 10.1371/journal.pone.0187544., eCollection 2017. PMID:29107991<ref>PMID:29107991</ref>
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Description: T48 deacetylase
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Rothweiler, U]]
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<div class="pdbe-citations 5lfz" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Arthrobacter sp. AW19M34-1]]
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[[Category: Large Structures]]
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[[Category: Rothweiler U]]

Current revision

T48 deacetylase

PDB ID 5lfz

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