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Structure paper

TitleThePlasmodium falciparumHsp70-x chaperone assists the heat stress response of the malaria parasite.
Journal, issue, pagesFaseb J., Vol. 33, Page 14611-14624, Year 2019
Publish dateJun 13, 2019 (structure data deposition date)
AuthorsDay, J. / Passecker, A. / Beck, H.P. / Vakonakis, I.
External linksFaseb J. / PubMed:31690116
MethodsX-ray diffraction
Resolution1.379 - 1.87 Å
Structure data

PDB-6rzq:
Plasmodium falciparum Hsp70-x chaperone nucleotide binding domain - ANP-PnP bound state
Method: X-RAY DIFFRACTION / Resolution: 1.81 Å

PDB-6rzy:
Plasmodium falciparum PFA0660w Hsp40 co-chaperone J-domain
Method: X-RAY DIFFRACTION / Resolution: 1.379 Å

PDB-6s02:
Plasmodium falciparum Hsp70-x chaperone nucleotide binding domain - ADP bound state
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • plasmodium falciparum (isolate 3d7) (eukaryote)
KeywordsCHAPERONE / Malaria Exported chaperone Intra-erythrocytic AMP-PnP / Malaria Exported co-chaperone Intra-erythrocytic / Malaria Exported chaperone Intra-erythrocytic ADP

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