5boe: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='5boe' size='340' side='right'caption='[[5boe]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='5boe' size='340' side='right'caption='[[5boe]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5boe]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5boe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BOE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BOE FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEP:PHOSPHOENOLPYRUVATE'>PEP</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEP:PHOSPHOENOLPYRUVATE'>PEP</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=5boe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5boe OCA], [https://pdbe.org/5boe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5boe RCSB], [https://www.ebi.ac.uk/pdbsum/5boe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5boe ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/ENO_STAAU ENO_STAAU] Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (By similarity). Binds laminin when expressed on the bacterial cell surface; this probably induces destruction of the extracellular matrix, favoring invasion and dissemination.[HAMAP-Rule:MF_00318]<ref>PMID:15158195</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 29: | Line 26: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Staphylococcus aureus]] | ||
[[Category: Han | [[Category: Han L]] | ||
[[Category: Wang | [[Category: Wang CL]] | ||
[[Category: Wu | [[Category: Wu MH]] | ||
[[Category: Wu | [[Category: Wu YF]] | ||
[[Category: Zang | [[Category: Zang JY]] | ||
[[Category: Zhang | [[Category: Zhang X]] | ||
Revision as of 09:01, 7 June 2023
Crystal structure of Staphylococcus aureus enolase in complex with PEPCrystal structure of Staphylococcus aureus enolase in complex with PEP
Structural highlights
FunctionENO_STAAU Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (By similarity). Binds laminin when expressed on the bacterial cell surface; this probably induces destruction of the extracellular matrix, favoring invasion and dissemination.[HAMAP-Rule:MF_00318][1] Publication Abstract from PubMedStaphylococcus aureus is a Gram-positive bacterium with strong pathogenicity that causes a wide range of infections and diseases. Enolase is an evolutionarily conserved enzyme that plays a key role in energy production through glycolysis. Additionally, enolase is located on the surface of S. aureus and is involved in processes leading to infection. Here, crystal structures of Sa_enolase with and without bound phosphoenolpyruvate (PEP) are presented at 1.6 and 2.45 A resolution, respectively. The structure reveals an octameric arrangement; however, both dimeric and octameric conformations were observed in solution. Furthermore, enzyme-activity assays show that only the octameric variant is catalytically active. Biochemical and structural studies indicate that the octameric form of Sa_enolase is enzymatically active in vitro and likely also in vivo, while the dimeric form is catalytically inactive and may be involved in other biological processes. Octameric structure of Staphylococcus aureus enolase in complex with phosphoenolpyruvate.,Wu Y, Wang C, Lin S, Wu M, Han L, Tian C, Zhang X, Zang J Acta Crystallogr D Biol Crystallogr. 2015 Dec 1;71(Pt 12):2457-70. doi:, 10.1107/S1399004715018830. Epub 2015 Nov 26. PMID:26627653[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||