Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2O2D

Crystal structure of phosphoglucose isomerase from Trypanosoma brucei complexed with citrate

Summary for 2O2D
Entry DOI10.2210/pdb2o2d/pdb
Related2O2D
DescriptorGlucose-6-phosphate isomerase, glycosomal, CITRIC ACID, GLYCEROL, ... (4 entities in total)
Functional Keywordsdimer, isomerase
Biological sourceTrypanosoma brucei brucei
Cellular locationGlycosome: P13377
Total number of polymer chains3
Total formula weight206228.62
Authors
Arsenieva, D.,Mazock, G.H.,Appavu, B.L.,Jeffery, C.J. (deposition date: 2006-11-29, release date: 2007-11-13, Last modification date: 2023-08-30)
Primary citationArsenieva, D.,Appavu, B.L.,Mazock, G.H.,Jeffery, C.J.
Crystal structure of phosphoglucose isomerase from Trypanosoma brucei complexed with glucose-6-phosphate at 1.6 A resolution
Proteins, 74:72-80, 2008
Cited by
PubMed Abstract: Enzymes of glycolysis in Trypanosoma brucei have been identified as potential drug targets for African sleeping sickness because glycolysis is the only source of ATP for the bloodstream form of this parasite. Several inhibitors were previously reported to bind preferentially to trypanosomal phosphoglucose isomerase (PGI, the second enzyme in glycolysis) than to mammalian PGIs, which suggests that PGI might make a good target for species-specific drug design. Herein, we report recombinant expression, purification, crystallization and X-ray crystal structure determination of T. brucei PGI. One structure solved at 1.6 A resolution contains a substrate, D-glucose-6-phosphate, in an extended conformation in the active site. A second structure solved at 1.9 A resolution contains a citrate molecule in the active site. The structures are compared with the crystal structures of PGI from humans and from Leishmania mexicana. The availability of recombinant tPGI and its first high-resolution crystal structures are initial steps in considering this enzyme as a potential drug target.
PubMed: 18561188
DOI: 10.1002/prot.22133
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

226707

数据于2024-10-30公开中

PDB statisticsPDBj update infoContact PDBjnumon