View source for 7pul


==Crystal structure of Endoglycosidase E GH20 domain from Enterococcus faecalis==
<StructureSection load='7pul' size='340' side='right'caption='[[7pul]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7pul]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PUL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PUL 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]] 1.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7pul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pul OCA], [https://pdbe.org/7pul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pul RCSB], [https://www.ebi.ac.uk/pdbsum/7pul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pul ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q839P8_ENTFA Q839P8_ENTFA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacteria produce a remarkably diverse range of glycoside hydrolases to metabolize glycans from the environment as a primary source of nutrients, and to promote the colonization and infection of a host. Here we focus on EndoE, a multi-modular glycoside hydrolase secreted by Enterococcus faecalis, one of the leading causes of healthcare-associated infections. We provide X-ray crystal structures of EndoE, which show an architecture composed of four domains, including GH18 and GH20 glycoside hydrolases connected by two consecutive three alpha-helical bundles. We determine that the GH20 domain is an exo-beta-1,2-N-acetylglucosaminidase, whereas the GH18 domain is an endo-beta-1,4-N-acetylglucosaminidase that exclusively processes the central core of complex-type or high-mannose-type N-glycans. Both glycoside hydrolase domains act in a concerted manner to process diverse N-glycans on glycoproteins, including therapeutic IgG antibodies. EndoE combines two enzyme domains with distinct functions and glycan specificities to play a dual role in glycan metabolism and immune evasion.

Mechanism of cooperative N-glycan processing by the multi-modular endoglycosidase EndoE.,Garcia-Alija M, Du JJ, Ordonez I, Diz-Vallenilla A, Moraleda-Montoya A, Sultana N, Huynh CG, Li C, Donahue TC, Wang LX, Trastoy B, Sundberg EJ, Guerin ME Nat Commun. 2022 Mar 3;13(1):1137. doi: 10.1038/s41467-022-28722-w. PMID:35241669<ref>PMID:35241669</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7pul" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Enterococcus faecalis]]
[[Category: Large Structures]]
[[Category: Du JJ]]
[[Category: Garcia-Alija M]]
[[Category: Guerin M]]
[[Category: Sundberg EJ]]
[[Category: Trastoy B]]