4chm | pdb_00004chm

Structure of Inner Membrane Complex (IMC) Sub-compartment Protein 1 (ISP1) from Toxoplasma gondii

spinqualitylabelsall models 4chm, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4chm is a 4 chain structure with sequence from Toxgm. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Related: 4chj Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Toxoplasma gondii, an apicomplexan parasite prevalent in developed nations, infects up to one third of the human population. The success of this parasite depends on several unique structures including an Inner Membrane Complex (IMC) that lines the interior of the plasma membrane and contains proteins important for gliding motility and replication. Of these proteins, the IMC Sub-compartment Proteins (ISPs) have recently been shown to play a role in asexual T. gondii daughter cell formation, yet the mechanism is unknown. Complicating mechanistic characterization of the ISPs is a lack of sequence identity with proteins of known structure or function. In support of elucidating the function of ISPs, we first determined the crystal structures of representative members TgISP1 and TgISP3 to a resolution of 2.10A and 2.32A, respectively. Structural analysis revealed that both ISPs adopt a Pleckstrin homology (PH) fold often associated with phospholipid binding or protein-protein interactions. Substitution of basic for hydrophobic residues in the region that overlays with phospholipid binding in related PH domains, however, suggests that ISPs do not retain phospholipid binding activity. Consistent with this observation, biochemical assays revealed no phospholipid binding activity. Interestingly, mapping of conserved surface residues combined with crystal packing analysis indicates that TgISPs have functionally repurposed the phospholipid-binding site likely to coordinate protein partners. Recruitment of larger protein complexes may also be aided through avidity-enhanced interactions resulting from multimerization of the ISPs. Overall, we propose a model where TgISPs recruit protein partners to the IMC to ensure correct progression of daughter cell formation. The inner membrane complex sub-compartment proteins critical for replication of the apicomplexan parasite Toxoplasma gondii adopt a Pleckstrin homology fold.,Tonkin ML, Beck JR, Bradley PJ, Boulanger MJ J Biol Chem. 2014 Mar 27. PMID:24675080 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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