Biochemical and structural characterization of residue 96 mutants of Plasmodium falciparum triosephosphate isomerase: active-site loop conformation, hydration and identification of a dimer-interface ligand-binding site.

Gayathri, P

Biochemical and structural characterization of residue 96 mutants of Plasmodium falciparum triosephosphate isomerase: active-site loop conformation, hydration and identification of a dimer-interface ligand-binding site. [electronic resource] - Acta crystallographica. Section D, Biological crystallography Aug 2009 - 847-57 p. digital

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

1399-0047

10.1107/S0907444909018666 doi


Animals
Catalytic Domain
Crystallization
Crystallography, X-Ray
Dimerization
Ligands
Mutant Proteins--chemistry
Phenylalanine--metabolism
Plasmodium falciparum--enzymology
Protein Binding
Protein Conformation
Protein Interaction Domains and Motifs
Protozoan Proteins--chemistry
Triose-Phosphate Isomerase--chemistry
Water