View source for 6en3


==Crystal structure of full length EndoS from Streptococcus pyogenes in complex with G2 oligosaccharide.==
<StructureSection load='6en3' size='340' side='right'caption='[[6en3]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6en3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibch Vibch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EN3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6EN3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rtxA, rtx, VC_1451 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6en3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6en3 OCA], [http://pdbe.org/6en3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6en3 RCSB], [http://www.ebi.ac.uk/pdbsum/6en3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6en3 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Endoglycosidase S (EndoS) is a bacterial endo-beta-N-acetylglucosaminidase that specifically catalyzes the hydrolysis of the beta-1,4 linkage between the first two N-acetylglucosamine residues of the biantennary complex-type N-linked glycans of IgG Fc regions. It is used for the chemoenzymatic synthesis of homogeneously glycosylated antibodies with improved therapeutic properties, but the molecular basis for its substrate specificity is unknown. Here, we report the crystal structure of the full-length EndoS in complex with its oligosaccharide G2 product. The glycoside hydrolase domain contains two well-defined asymmetric grooves that accommodate the complex-type N-linked glycan antennae near the active site. Several loops shape the glycan binding site, thereby governing the strict substrate specificity of EndoS. Comparing the arrangement of these loops within EndoS and related endoglycosidases, reveals distinct-binding site architectures that correlate with the respective glycan specificities, providing a basis for the bioengineering of endoglycosidases to tailor the chemoenzymatic synthesis of monoclonal antibodies.

Structural basis for the recognition of complex-type N-glycans by Endoglycosidase S.,Trastoy B, Klontz E, Orwenyo J, Marina A, Wang LX, Sundberg EJ, Guerin ME Nat Commun. 2018 May 14;9(1):1874. doi: 10.1038/s41467-018-04300-x. PMID:29760474<ref>PMID:29760474</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6en3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibch]]
[[Category: Guerin, M E]]
[[Category: Klontz, E H]]
[[Category: Marina, A]]
[[Category: Orwenyo, J]]
[[Category: Sundberg, E J]]
[[Category: Trastoy, B]]
[[Category: Wang, L X]]
[[Category: Endoglycosidase/immunoglobulin/carbohydrate/endo-beta-n-acetylglucos aminidase]]
[[Category: Hydrolase]]