2yl8: Difference between revisions

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[[Image:2yl8.jpg|left|200px]]


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==Inhibition of the pneumococcal virulence factor StrH and molecular insights into N-glycan recognition and hydrolysis==
The line below this paragraph, containing "STRUCTURE_2yl8", creates the "Structure Box" on the page.
<StructureSection load='2yl8' size='340' side='right'caption='[[2yl8]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2yl8]] is a 1 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=2YL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YL8 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=15P:POLYETHYLENE+GLYCOL+(N=34)'>15P</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
{{STRUCTURE_2yl8|  PDB=2yl8  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2yl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yl8 OCA], [https://pdbe.org/2yl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yl8 RCSB], [https://www.ebi.ac.uk/pdbsum/2yl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yl8 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===
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2yl8" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
[[2yl8]] 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=2YL8 OCA].
*[[Beta-Hexosaminidase|Beta-Hexosaminidase]]
[[Category: Beta-N-acetylhexosaminidase]]
*[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]]
[[Category: Streptococcus pneumoniae]]
*[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]]
[[Category: Abbott, W D.]]
== References ==
[[Category: Boraston, A B.]]
<references/>
[[Category: Dalia, A B.]]
__TOC__
[[Category: Deng, L.]]
</StructureSection>
[[Category: Fairbanks, A J.]]
[[Category: Large Structures]]
[[Category: Higgins, M A.]]
[[Category: Streptococcus pneumoniae TIGR4]]
[[Category: Parsons, T B.]]
[[Category: Abbott DW]]
[[Category: Pluvinage, B.]]
[[Category: Boraston AB]]
[[Category: Robb, C.]]
[[Category: Dalia AB]]
[[Category: Vocadlo, D J.]]
[[Category: Deng L]]
[[Category: Weiser, J N.]]
[[Category: Fairbanks AJ]]
[[Category: Hydrolase]]
[[Category: Higgins MA]]
[[Category: Parsons TB]]
[[Category: Pluvinage B]]
[[Category: Robb C]]
[[Category: Vocadlo DJ]]
[[Category: Weiser JN]]

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

2yl8 is a 1 chain structure with sequence from Streptococcus pneumoniae TIGR4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.75Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

STRH_STRPN

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Pluvinage B, Higgins MA, Abbott DW, Robb C, Dalia AB, Deng L, Weiser JN, Parsons TB, Fairbanks AJ, Vocadlo DJ, Boraston AB. Inhibition of the Pneumococcal Virulence Factor StrH and Molecular Insights into N-Glycan Recognition and Hydrolysis. Structure. 2011 Nov 9;19(11):1603-14. PMID:22078560 doi:10.1016/j.str.2011.08.011

2yl8, resolution 1.75Å

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