Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: Observation of the catalytic loop in the open conformation in the ligand-bound state

S. Parthasarathy, Hemalatha Balaram, P. Balaram, M. R.N. Murthy

Research output: Contribution to journalArticle

22 Scopus citations

Abstract

Structures of triosephosphate isomerase (TIM) from the malarial parasite P. falciparum (Pf) complexed to the substrate analogues 3-phosphoglycerate and glycerol-3-phosphate have been determined at 2.4 Å resolution. The catalytic loop of TIM adopts a novel 'loop-open' conformation in these complexes. These structures provide insight into the design of inhibitors specific for the malarial enzyme.

Original languageEnglish (US)
Pages (from-to)1992-2000
Number of pages9
JournalActa Crystallographica Section D: Biological Crystallography
Volume58
Issue number12
DOIs
StatePublished - Dec 1 2002

ASJC Scopus subject areas

  • Structural Biology

Fingerprint Dive into the research topics of 'Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: Observation of the catalytic loop in the open conformation in the ligand-bound state'. Together they form a unique fingerprint.

  • Cite this