2yla: Difference between revisions
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< | ==INHIBITION OF THE PNEUMOCOCCAL VIRULENCE FACTOR STRH AND MOLECULAR INSIGHTS INTO N-GLYCAN RECOGNITION AND HYDROLYSIS== | ||
<StructureSection load='2yla' size='340' side='right'caption='[[2yla]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2yla]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_TIGR4 Streptococcus pneumoniae TIGR4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YLA 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]] 2.7Å</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=2yla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yla OCA], [https://pdbe.org/2yla PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yla RCSB], [https://www.ebi.ac.uk/pdbsum/2yla PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yla ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/STRH_STRPN STRH_STRPN] | |||
<div style="background-color:#fffaf0;"> | |||
== 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 MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2yla" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-Hexosaminidase|Beta-Hexosaminidase]] | |||
*[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]] | |||
*[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]] | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
[[ | </StructureSection> | ||
[[Category: Large Structures]] | |||
== | [[Category: Streptococcus pneumoniae TIGR4]] | ||
< | [[Category: Abbott DW]] | ||
[[Category: | [[Category: Boraston AB]] | ||
[[Category: Streptococcus pneumoniae]] | [[Category: Dalia AB]] | ||
[[Category: Abbott | [[Category: Deng L]] | ||
[[Category: Boraston | [[Category: Fairbanks AJ]] | ||
[[Category: Dalia | [[Category: Higgins MA]] | ||
[[Category: Deng | [[Category: Parsons TB]] | ||
[[Category: Fairbanks | [[Category: Pluvinage B]] | ||
[[Category: Higgins | [[Category: Robb C]] | ||
[[Category: Parsons | [[Category: Vocadlo DJ]] | ||
[[Category: Pluvinage | [[Category: Weiser JN]] | ||
[[Category: Robb | |||
[[Category: Vocadlo | |||
[[Category: Weiser | |||
Latest revision as of 17:05, 1 February 2024
INHIBITION OF THE PNEUMOCOCCAL VIRULENCE FACTOR STRH AND MOLECULAR INSIGHTS INTO N-GLYCAN RECOGNITION AND HYDROLYSISINHIBITION OF THE PNEUMOCOCCAL VIRULENCE FACTOR STRH AND MOLECULAR INSIGHTS INTO N-GLYCAN RECOGNITION AND HYDROLYSIS
Structural highlights
FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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