Application | Comment | Organism |
---|---|---|
drug development | reconstitution of the entire Plasmodium translocon of exported proteins, PTEX, to aid structure-based design of anti-malarial drugs | Plasmodium falciparum |
Crystallization (Comment) | Organism |
---|---|
purified isolated N-terminal domains of ClpB1 bound to GFP, ClpB1-sfGFP, X-ray diffraction structure determination and analysis at 1.8 A resolution | Plasmodium falciparum |
purified isolated N-terminal domains of ClpB1, X-ray diffraction structure determination and analysis at 1.65-2.01 A resolution | Plasmodium falciparum |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
apicoplast | - |
Plasmodium falciparum | 20011 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Plasmodium falciparum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | Plasmodium falciparum | - |
ADP + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Plasmodium falciparum | - |
- |
- |
Plasmodium falciparum | A0A0L7LXM6 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | - |
Plasmodium falciparum | ADP + phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
hexamer | - |
Plasmodium falciparum |
Synonyms | Comment | Organism |
---|---|---|
ClpB ATPase | - |
Plasmodium falciparum |
ClpB1 | - |
Plasmodium falciparum |
ClpB2 | - |
Plasmodium falciparum |
ClpB2/HSP101 | - |
Plasmodium falciparum |
HSP101 | - |
Plasmodium falciparum |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the class 1 Clp AAA1 proteins of the superfamily of AAA+ proteins harboring signature Walker A and B motifs | Plasmodium falciparum |
malfunction | ablation or inactivation of HSP101/ClpB2 in parasites results in the nearly complete block in export with substrates accumulating in the vacuole;33 furthermore this blockade affects all classes of exported proteins, whether they harbor a PEXEL motif or not | Plasmodium falciparum |
additional information | ClpB proteins share a common architecture consisting of four domains, a variable N-terminal domain that binds different protein substrates, followed by two highly conserved catalytic ATPase domains, and a C-terminal domain, structure overview. Pseudo two-fold internal symmetry creates a hydrophobic patch at the surface of the N terminal domains of the two ClpB chaperones from Plasmodium | Plasmodium falciparum |
physiological function | ClpB proteins function as unfoldases and disaggregases. ClpB1 is present in the apicoplast, a parasite-specific and plastid-like organelle hosting various metabolic pathways necessary for parasite growth. Molecular chaperones appear to play important roles in keeping parasite proteins in a translocation competent state prior to crossing the parasitophorous vacuole membrane | Plasmodium falciparum |
physiological function | ClpB proteins function as unfoldases and disaggregases. ClpB2 localizes to the parasitophorous vacuole membrane where it drives protein export as core subunit of a parasite-derived protein secretion complex, the Plasmodium translocon of exported proteins (PTEX), this process is central to parasite virulence and survival in the human host. Molecular chaperones appear to play important roles in keeping parasite proteins in a translocation competent state prior to crossing the parasitophorous vacuole membrane. ClpB2/HSP101 is essential to the organism and actively drives the export process by harnessing the energy from ATP hydrolysis to unfold and thread the diverse cargos through the trans-membrane conduit EXP2 | Plasmodium falciparum |