1O5X

Plasmodium falciparum TIM complexed to 2-phosphoglycerate

Summary for 1O5X

• Entry DOI: 10.2210/pdb1o5x/pdb
• Descriptor: Triosephosphate isomerase, PHOSPHITE ION, 3-HYDROXYPYRUVIC ACID, ... (5 entities in total)
• Functional Keywords: triosephosphate isomerase, plasmodium falciparum, 2-phosphoglycerate, meta-phosphate, catalytic loop6, isomerase
• Biological source: Plasmodium falciparum (malaria parasite P. falciparum)
• Total number of polymer chains: 2
• Total formula weight: 56364.57

Authors

Parthasarathy, S.,Eaazhisai, K.,Balaram, H.,Balaram, P.,Murthy, M.R. (deposition date: 2003-10-06, release date: 2004-01-13, Last modification date: 2024-12-25)

Primary citation

Parthasarathy, S.,Eaazhisai, K.,Balaram, H.,Balaram, P.,Murthy, M.R.
Structure of Plasmodium falciparum Triose-phosphate Isomerase-2-Phosphoglycerate Complex at 1.1-A Resolution
J.Biol.Chem., 278:52461-52470, 2003

PubMed Abstract: Triose-phosphate isomerase, a key enzyme of the glycolytic pathway, catalyzes the isomerization of dihydroxy acetone phosphate and glyceraldehyde 3-phosphate. In this communication we report the crystal structure of Plasmodium falciparum triose-phosphate isomerase complexed to the inhibitor 2-phosphoglycerate at 1.1-A resolution. The crystallographic asymmetric unit contains a dimeric molecule. The inhibitor bound to one of the subunits in which the flexible catalytic loop 6 is in the open conformation has been cleaved into two fragments presumably due to radiation damage. The cleavage products have been tentatively identified as 2-oxoglycerate and meta-phosphate. The intact 2-phosphoglycerate bound to the active site of the other subunit has been observed in two different orientations. The active site loop in this subunit is in both open and "closed" conformations, although the open form is predominant. Concomitant with the loop closure, Phe-96, Leu-167, and residues 208-211 (YGGS) are also observed in dual conformations in the B-subunit. Detailed comparison of the active-site geometry in the present case to the Saccharomyces cerevisiae triose-phosphate isomerase-dihydroxy acetone phosphate and Leishmania mexicana triose-phosphate isomerase-phosphoglycolate complexes, which have also been determined at atomic resolution, shows that certain interactions are common to the three structures, although 2-phosphoglycerate is neither a substrate nor a transition state analogue.

PubMed: 14563846
DOI: 10.1074/jbc.M308525200

Experimental method

X-RAY DIFFRACTION (1.1 Å)