7rhw
From Proteopedia
(Difference between revisions)
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==Aspergillus fumigatus Enolase Bound to 2-Phosphoglycerate== | ==Aspergillus fumigatus Enolase Bound to 2-Phosphoglycerate== | ||
| - | <StructureSection load='7rhw' size='340' side='right'caption='[[7rhw]]' scene=''> | + | <StructureSection load='7rhw' size='340' side='right'caption='[[7rhw]], [[Resolution|resolution]] 1.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RHW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RHW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7rhw]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RHW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RHW FirstGlance]. <br> |
| - | </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=7rhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rhw OCA], [https://pdbe.org/7rhw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rhw RCSB], [https://www.ebi.ac.uk/pdbsum/7rhw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rhw ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2PG:2-PHOSPHOGLYCERIC+ACID'>2PG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7rhv|7rhv]]</div></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] </span></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=7rhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rhw OCA], [https://pdbe.org/7rhw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rhw RCSB], [https://www.ebi.ac.uk/pdbsum/7rhw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rhw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The metabolic enzyme, enolase, plays a crucial role in the cytoplasm where it maintains cellular energy production within the process of glycolysis. The main role of enolase in glycolysis is to convert 2-phosphoglycerate to phosphoenolpyruvate; however, enolase can fulfil roles that deviate from this function. In pathogenic bacteria and fungi, enolase is also located on the cell surface where it functions as a virulence factor. Surface-expressed enolase is a receptor for human plasma proteins, including plasminogen, and this interaction facilitates nutrient acquisition and tissue invasion. A novel approach to developing antifungal drugs is to inhibit the formation of this complex. To better understand the structure of enolase and the interactions that may govern complex formation, we have solved the first X-ray crystal structure of enolase from A. fumigatus (2.0 A) and have shown that it preferentially adopts a dimeric quaternary structure using native mass spectrometry. Two additional X-ray crystal structures of A. fumigatus enolase bound to the endogenous substrate 2-phosphoglycerate and product phosphoenolpyruvate were determined. Kinetic characterization was carried out to better understand the details of its canonical function. From these data, we have produced a model of the A. fumigatus enolase and human plasminogen complex to provide structural insights into mechanisms of virulence and future development of small molecules or peptidomimetics for anti-fungal drug design. This article is protected by copyright. All rights reserved. | ||
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| + | A structural model of the human plasminogen and Aspergillus fumigatus enolase complex.,Nguyen S, Jovcevski B, Truong JQ, Pukala TL, Bruning JB Proteins. 2022 Mar 5. doi: 10.1002/prot.26331. PMID:35247004<ref>PMID:35247004</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7rhw" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Bruning | + | [[Category: Phosphopyruvate hydratase]] |
| - | [[Category: Nguyen S]] | + | [[Category: Bruning, J B]] |
| + | [[Category: Nguyen, S]] | ||
| + | [[Category: Glycolysis]] | ||
| + | [[Category: Lyase]] | ||
Revision as of 07:10, 20 July 2022
Aspergillus fumigatus Enolase Bound to 2-Phosphoglycerate
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