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Structure paper

TitleProminent role of cysteine residues C49 and C343 in regulating Plasmodium falciparum pyruvate kinase activity.
Journal, issue, pagesStructure, Vol. 30, Page 1452-, Year 2022
Publish dateMar 4, 2022 (structure data deposition date)
AuthorsDillenberger, M. / Rahlfs, S. / Becker, K. / Fritz-Wolf, K.
External linksStructure / PubMed:35998635
MethodsX-ray diffraction
Resolution1.8 - 2.1 Å
Structure data

PDB-7z4m:
Plasmodium falciparum pyruvate kinase complexed with Mg2+ and K+
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-7z4n:
Plasmodium falciparum pyruvate kinase complexed with pyruvate
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-7z4q:
Plasmodium falciparum pyruvate kinase mutant - C49A
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-7z4r:
Plasmodium falciparum pyruvate kinase mutant - C343A
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

ChemComp-PYR:
PYRUVIC ACID

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

Source
  • plasmodium falciparum 3d7 (eukaryote)
KeywordsTRANSFERASE / Redox regulation / glycolysis / malaria / drug-target

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