1O5X

Plasmodium falciparum TIM complexed to 2-phosphoglycerate

1O5X の概要

• エントリーDOI: 10.2210/pdb1o5x/pdb
• 分子名称: Triosephosphate isomerase, PHOSPHITE ION, 3-HYDROXYPYRUVIC ACID, ... (5 entities in total)
• 機能のキーワード: triosephosphate isomerase, plasmodium falciparum, 2-phosphoglycerate, meta-phosphate, catalytic loop6, isomerase
• 由来する生物種: Plasmodium falciparum (malaria parasite P. falciparum)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56364.57

構造登録者

Parthasarathy, S.,Eaazhisai, K.,Balaram, H.,Balaram, P.,Murthy, M.R. (登録日: 2003-10-06, 公開日: 2004-01-13, 最終更新日: 2024-12-25)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.1 Å)