4ewj: Difference between revisions
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==structure of the enloase from Streptococcus suis serotype 2== | |||
<StructureSection load='4ewj' size='340' side='right'caption='[[4ewj]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ewj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_suis Streptococcus suis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EWJ 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]] 2.403Å</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=4ewj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ewj OCA], [https://pdbe.org/4ewj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ewj RCSB], [https://www.ebi.ac.uk/pdbsum/4ewj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ewj ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/K7N5M7_STRSU K7N5M7_STRSU] Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.[HAMAP-Rule:MF_00318] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Enolase is a conserved cytoplasmic metalloenzyme existing universally in both eukaryotic and prokaryotic cells. The enzyme can also locate on the cell surface and bind to plasminogen, via which contributing to the mucosal surface localization of the bacterial pathogens and assisting the invasion into the host cells. The functions of the eukaryotic enzymes on the cell surface expression (including T cells, B cells, neutrophils, monocytoes, neuronal cells and epithelial cells) are not known. Streptococcus suis serotype 2 (S. suis 2, SS2) is an important zoonotic pathogen which has recently caused two large-scale outbreaks in southern China with severe streptococcal toxic shock syndrome (STSS) never seen before in human sufferers. We recently identified the SS2 enolase as an important protective antigen which could protect mice from fatal S.suis 2 infection. In this study, a 2.4-angstrom structure of the SS2 enolase is solved, revealing an octameric arrangement in the crystal. We further demonstrated that the enzyme exists exclusively as an octamer in solution via a sedimentation assay. These results indicate that the octamer is the biological unit of SS2 enolase at least in vitro and most likely in vivo as well. This is, to our knowledge, the first comprehensive characterization of the SS2 enolase octamer both structurally and biophysically, and the second octamer enolase structure in addition to that of Streptococcus pneumoniae. We also investigated the plasminogen binding property of the SS2 enzyme. | |||
An octamer of enolase from Streptococcus suis.,Lu Q, Lu H, Qi J, Lu G, Gao GF Protein Cell. 2012 Oct;3(10):769-80. doi: 10.1007/s13238-012-2040-7. Epub 2012, Oct 11. PMID:23055041<ref>PMID:23055041</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4ewj" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Enolase 3D structures|Enolase 3D structures]] | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus suis]] | [[Category: Streptococcus suis]] | ||
[[Category: Gao | [[Category: Gao GF]] | ||
[[Category: Lu | [[Category: Lu G]] | ||
[[Category: Lu | [[Category: Lu H]] | ||
[[Category: Lu | [[Category: Lu Q]] | ||
[[Category: Qi | [[Category: Qi J]] | ||
Latest revision as of 16:50, 8 November 2023
structure of the enloase from Streptococcus suis serotype 2structure of the enloase from Streptococcus suis serotype 2
Structural highlights
FunctionK7N5M7_STRSU Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.[HAMAP-Rule:MF_00318] Publication Abstract from PubMedEnolase is a conserved cytoplasmic metalloenzyme existing universally in both eukaryotic and prokaryotic cells. The enzyme can also locate on the cell surface and bind to plasminogen, via which contributing to the mucosal surface localization of the bacterial pathogens and assisting the invasion into the host cells. The functions of the eukaryotic enzymes on the cell surface expression (including T cells, B cells, neutrophils, monocytoes, neuronal cells and epithelial cells) are not known. Streptococcus suis serotype 2 (S. suis 2, SS2) is an important zoonotic pathogen which has recently caused two large-scale outbreaks in southern China with severe streptococcal toxic shock syndrome (STSS) never seen before in human sufferers. We recently identified the SS2 enolase as an important protective antigen which could protect mice from fatal S.suis 2 infection. In this study, a 2.4-angstrom structure of the SS2 enolase is solved, revealing an octameric arrangement in the crystal. We further demonstrated that the enzyme exists exclusively as an octamer in solution via a sedimentation assay. These results indicate that the octamer is the biological unit of SS2 enolase at least in vitro and most likely in vivo as well. This is, to our knowledge, the first comprehensive characterization of the SS2 enolase octamer both structurally and biophysically, and the second octamer enolase structure in addition to that of Streptococcus pneumoniae. We also investigated the plasminogen binding property of the SS2 enzyme. An octamer of enolase from Streptococcus suis.,Lu Q, Lu H, Qi J, Lu G, Gao GF Protein Cell. 2012 Oct;3(10):769-80. doi: 10.1007/s13238-012-2040-7. Epub 2012, Oct 11. PMID:23055041[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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