8DE5

Structure of glyceraldehyde-3-phosphate dehydrogenase from Paracoccidioides lutzii

Summary for 8DE5

• Entry DOI: 10.2210/pdb8de5/pdb
• Descriptor: Glyceraldehyde-3-phosphate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, D-galactonic acid, ... (6 entities in total)
• Functional Keywords: glyceraldehyde-3-phosphate dehydrogenase, paracoccidioides lutzii, paracoccidioidomycosis, aldonic sugar acid, oxidoreductase
• Biological source: Paracoccidioides lutzii Pb01
• Total number of polymer chains: 1
• Total formula weight: 38056.57

Authors

Hernandez-Prieto, J.H.,Martini, V.P.,Iulek, J. (deposition date: 2022-06-19, release date: 2023-06-21, Last modification date: 2024-11-13)

Primary citation

Hernandez-Prieto, J.H.,Martini, V.P.,Iulek, J.
Structure of glyceraldehyde-3-phosphate dehydrogenase from Paracoccidioides lutzii in complex with an aldonic sugar acid.
Biochimie, 218:20-33, 2023

PubMed Abstract: The pathogen Paracoccidioides lutzii (Pb01) is found in South America countries Colombia, Ecuador, Venezuela and Brazil, especially in the central, west, and north regions of the latter. It belongs to the Ajellomycetaceae family, Onygenales order, and is typically thermodimorphic, presenting yeast cells when it grows in animal tissues, but mycelia when in the environment, where it produces the infectious propagule. This fungus is one of the etiologic agents of Paracoccidioidomycosis (PCM), the most important endemic fungal infection in Latin America. Investigations on its genome have contributed to a better understanding about its metabolism and revealed the complexity of several metabolic glycolytic pathways. Glyceraldehyde-3-Phosphate Dehydrogenase from Paracoccidioides lutzii (PlGAPDH) is considered a moonlighting protein and participates in several biological processes of this pathogen. The enzyme was expressed and purified, as seen in SDS-PAGE gel, crystallized and had its three dimensional structure (3D) determined in complex with NAD, a sulphate ion and d-galactonic acid, therefore, a type of 'GAA site'. It is the first GAPDH structure to show this chemical type in this site and how this protein can bind an acid derived from oxidation of a linear hexose.

PubMed: 37709188
DOI: 10.1016/j.biochi.2023.09.013

Experimental method

X-RAY DIFFRACTION (2.02 Å)