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 Citations (Scopus)

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
Externally publishedYes

Fingerprint

Triose-Phosphate Isomerase
Plasmodium falciparum
Conformations
Observation
analogs
Ligands
parasites
ligands
Substrates
glycerols
inhibitors
enzymes
phosphates
Parasites
Enzymes
alpha-glycerophosphoric acid
3-phosphoglycerate

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

Cite this

Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues : Observation of the catalytic loop in the open conformation in the ligand-bound state. / Parthasarathy, S.; Balaram, Hemalatha; Balaram, P.; Murthy, M. R N.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 58, No. 12, 01.12.2002, p. 1992-2000.

Research output: Contribution to journalArticle

@article{d0e1d4db854646a29deb662e656b239b,
title = "Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: Observation of the catalytic loop in the open conformation in the ligand-bound state",
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 {\AA} 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.",
author = "S. Parthasarathy and Hemalatha Balaram and P. Balaram and Murthy, {M. R N}",
year = "2002",
month = "12",
day = "1",
doi = "10.1107/S0907444902015433",
language = "English (US)",
volume = "58",
pages = "1992--2000",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "0907-4449",
publisher = "John Wiley and Sons Inc.",
number = "12",

}

TY - JOUR

T1 - Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues

T2 - Observation of the catalytic loop in the open conformation in the ligand-bound state

AU - Parthasarathy, S.

AU - Balaram, Hemalatha

AU - Balaram, P.

AU - Murthy, M. R N

PY - 2002/12/1

Y1 - 2002/12/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0036899889&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036899889&partnerID=8YFLogxK

U2 - 10.1107/S0907444902015433

DO - 10.1107/S0907444902015433

M3 - Article

C2 - 12454456

AN - SCOPUS:0036899889

VL - 58

SP - 1992

EP - 2000

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 0907-4449

IS - 12

ER -