7ri0 | pdb_00007ri0

Aspergillus fumigatus Enolase Bound to Phosphoenolpyruvate and 2-Phosphoglycerate

spinqualitylabelsall models 7ri0, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7ri0 is a 2 chain structure with sequence from Aspergillus fumigatus Af293. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: 2PG, MG, PEP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ENO_ASPFU 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Enolase 3D structures

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