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< | ==Crystal Structure of the Streptococcus pyogenes NAD+ glycohydrolase SPN in complex with IFS, the Immunity Factor for SPN== | ||
<StructureSection load='3pnt' size='340' side='right'caption='[[3pnt]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3pnt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PNT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PNT 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]] 2.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3pnt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pnt OCA], [https://pdbe.org/3pnt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pnt RCSB], [https://www.ebi.ac.uk/pdbsum/3pnt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pnt ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/D7S065_STRPY D7S065_STRPY] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The virulence of Gram-positive bacteria is enhanced by toxins like the Streptococcus pyogenes beta-NAD(+) glycohydrolase known as SPN. SPN-producing strains of S. pyogenes additionally express the protein immunity factor for SPN (IFS), which forms an inhibitory complex with SPN. We have determined crystal structures of the SPN-IFS complex and IFS alone, revealing that SPN is structurally related to ADP-ribosyl transferases but lacks the canonical binding site for protein substrates. SPN is instead a highly efficient glycohydrolase with the potential to deplete cellular levels of beta-NAD(+). The protective effect of IFS involves an extensive interaction with the SPN active site that blocks access to beta-NAD(+). The conformation of IFS changes upon binding to SPN, with repacking of an extended C-terminal alpha helix into a compact shape. IFS is an attractive target for the development of novel bacteriocidal compounds functioning by blocking the bacterium's self-immunity to the SPN toxin. | |||
Structural Basis of Streptococcus pyogenes Immunity to Its NAD(+) Glycohydrolase Toxin.,Smith CL, Ghosh J, Elam JS, Pinkner JS, Hultgren SJ, Caparon MG, Ellenberger T Structure. 2011 Feb 9;19(2):192-202. PMID:21300288<ref>PMID:21300288</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3pnt" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: Streptococcus pyogenes]] | [[Category: Streptococcus pyogenes]] | ||
[[Category: Caparon | [[Category: Caparon MG]] | ||
[[Category: | [[Category: Ellenberger T]] | ||
[[Category: | [[Category: Ghosh J]] | ||
[[Category: | [[Category: Hultgren SJ]] | ||
[[Category: | [[Category: Pinkner JS]] | ||
[[Category: | [[Category: Smith CL]] | ||
[[Category: | [[Category: Stine Elam J]] | ||
Latest revision as of 09:39, 27 November 2024
Crystal Structure of the Streptococcus pyogenes NAD+ glycohydrolase SPN in complex with IFS, the Immunity Factor for SPNCrystal Structure of the Streptococcus pyogenes NAD+ glycohydrolase SPN in complex with IFS, the Immunity Factor for SPN
Structural highlights
FunctionPublication Abstract from PubMedThe virulence of Gram-positive bacteria is enhanced by toxins like the Streptococcus pyogenes beta-NAD(+) glycohydrolase known as SPN. SPN-producing strains of S. pyogenes additionally express the protein immunity factor for SPN (IFS), which forms an inhibitory complex with SPN. We have determined crystal structures of the SPN-IFS complex and IFS alone, revealing that SPN is structurally related to ADP-ribosyl transferases but lacks the canonical binding site for protein substrates. SPN is instead a highly efficient glycohydrolase with the potential to deplete cellular levels of beta-NAD(+). The protective effect of IFS involves an extensive interaction with the SPN active site that blocks access to beta-NAD(+). The conformation of IFS changes upon binding to SPN, with repacking of an extended C-terminal alpha helix into a compact shape. IFS is an attractive target for the development of novel bacteriocidal compounds functioning by blocking the bacterium's self-immunity to the SPN toxin. Structural Basis of Streptococcus pyogenes Immunity to Its NAD(+) Glycohydrolase Toxin.,Smith CL, Ghosh J, Elam JS, Pinkner JS, Hultgren SJ, Caparon MG, Ellenberger T Structure. 2011 Feb 9;19(2):192-202. PMID:21300288[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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