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Literature summary for 3.6.4.10 extracted from

  • AhYoung, A.P.; Koehl, A.; Cascio, D.; Egea, P.F.
    Structural mapping of the ClpB ATPases of Plasmodium falciparum: Targeting protein folding and secretion for antimalarial drug design (2015), Protein Sci., 24, 1508-1520.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.10

Application

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 (Commentary)

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

Localization Comment Organism GeneOntology No. Textmining
apicoplast
-
 Plasmodium falciparum 20011
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Plasmodium falciparum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Plasmodium falciparum
-
 ADP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-
Plasmodium falciparum A0A0L7LXM6
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Plasmodium falciparum ADP + phosphate
-
 ?

Subunits

Subunits Comment Organism
hexamer
-
 Plasmodium falciparum

Synonyms

Synonyms Comment Organism
ClpB ATPase
-
 Plasmodium falciparum
ClpB1
-
 Plasmodium falciparum
ClpB2
-
 Plasmodium falciparum
ClpB2/HSP101
-
 Plasmodium falciparum
HSP101
-
 Plasmodium falciparum

General Information

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