View source for 2yll

==INHIBITION OF THE PNEUMOCOCCAL VIRULENCE FACTOR STRH AND MOLECULAR INSIGHTS INTO N-GLYCAN RECOGNITION AND HYDROLYSIS==
<StructureSection load='2yll' size='340' side='right' caption='[[2yll]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2yll]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YLL OCA]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yl6|2yl6]], [[2yl9|2yl9]], [[2yl5|2yl5]], [[2yla|2yla]], [[2yl8|2yl8]]</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yll OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yll RCSB], [http://www.ebi.ac.uk/pdbsum/2yll PDBsum]</span></td></tr>
<table>
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== Publication Abstract from PubMed ==
The complete degradation of N-linked glycans by the pathogenic bacterium Streptococcus pneumoniae is facilitated by the large multimodular cell wall-attached exo-beta-D-N-acetylglucosaminidase StrH. Structural dissection of this virulence factor using X-ray crystallography showed it to have two structurally related glycoside hydrolase family 20 catalytic domains, which displayed the expected specificity for complex N-glycans terminating in N-acetylglucosamine but exhibited unexpected differences in their preferences for the substructures present in these glycans. The structures of the two catalytic domains in complex with unhydrolyzed substrates, including an N-glycan possessing a bisecting N-acetylglucosamine residue, revealed the specific architectural features in the active sites that confer their differential specificities. Inhibitors of StrH are demonstrated to be effective tools in modulating the interaction of StrH with components of the host, such as the innate immune system. Overall, new structural and functional insight into a carbohydrate-mediated component of the pneumococcus-host interaction is provided.

Inhibition of the Pneumococcal Virulence Factor StrH and Molecular Insights into N-Glycan Recognition and Hydrolysis.,Pluvinage B, Higgins MA, Abbott DW, Robb C, Dalia AB, Deng L, Weiser JN, Parsons TB, Fairbanks AJ, Vocadlo DJ, Boraston AB Structure. 2011 Nov 9;19(11):1603-14. PMID:22078560<ref>PMID:22078560</ref>

From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Beta-N-acetylhexosaminidase]]
[[Category: Streptococcus pneumoniae]]
[[Category: Abbott, D W.]]
[[Category: Boraston, A B.]]
[[Category: Dalia, A B.]]
[[Category: Deng, L.]]
[[Category: Fairbanks, A J.]]
[[Category: Higgins, M A.]]
[[Category: Parsons, T B.]]
[[Category: Pluvinage, B.]]
[[Category: Robb, C.]]
[[Category: Vocadlo, D J.]]
[[Category: Weiser, J N.]]
[[Category: Hydrolase]]