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'''Unreleased structure'''


The entry 3wwg is ON HOLD  until Paper Publication
==Crystal structure of the N-glycan-deficient variant N448A of isopullulanase complexed with isopanose==
<StructureSection load='3wwg' size='340' side='right'caption='[[3wwg]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wwg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WWG 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</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=3wwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wwg OCA], [https://pdbe.org/3wwg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wwg RCSB], [https://www.ebi.ac.uk/pdbsum/3wwg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wwg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IPUA_ASPNG IPUA_ASPNG] Hydrolyzes pullulan, a linear polymer which is composed of maltotriose units with alpha-1,6 glucosidic linkages, to produce isopanose (Glca1-4Glca1-6Glc).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
N-glycosylation has been shown to be important for the stability of some glycoproteins. Isopullulanase (IPU), a polysaccharide-hydrolyzing enzyme, is a highly N-glycosylated protein, and IPU deglycosylation results in a decrease in thermostability. To investigate the function of N-glycan in IPU, we focused on an N-glycosylated residue located in the vicinity of the active site, Asn448. The thermostabilities of three IPU variants, Y440A, N448A and S450A, were 0.5-8.4 degrees C lower than the wild-type enzyme. The crystal structure of endoglycosidase H (Endo H)-treated N448A variant was determined. There are four IPU molecules, Mol-A, B, C and D, in the asymmetric unit. The conformation of a loop composed of amino acid residues 435-455 in Mol-C was identical to wild-type IPU, whereas the conformations of this loop in Mol-A, Mol-B and Mol-D were different from each other. These results suggest that the Asn448 side chain is primarily important for the stability of IPU. Our results indicate that mutation of only N-glycosylated Asn residue may lead to incorrect conclusion for the evaluation of the function of N-glycan. Usually, the structures of N-glycosylation sites form an extended configuration in IPU; however, the Asn448 site had an atypical structure that lacked this configuration.


Authors: Miyazaki, T., Yashiro, H., Nishikawa, A., Tonozuka, T.
The side chain of a glycosylated asparagine residue is important for the stability of isopullulanase.,Miyazaki T, Yashiro H, Nishikawa A, Tonozuka T J Biochem. 2015 Apr;157(4):225-34. doi: 10.1093/jb/mvu065. Epub 2014 Oct 29. PMID:25359784<ref>PMID:25359784</ref>


Description: Crystal structure of the N-glycan-deficient variant N448A of isopullulanase complexed with isopanose
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wwg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aspergillus niger]]
[[Category: Large Structures]]
[[Category: Miyazaki T]]
[[Category: Nishikawa A]]
[[Category: Tonozuka T]]
[[Category: Yashiro H]]
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