Publication Date:
2012-06-28
Description:
The protozoan parasites of the Apicomplexa phylum are devastating global pathogens. Their success is largely due to phylum-specific proteins found in specialized organelles and cellular structures. The inner membrane complex (IMC) is a unique apicomplexan structure that is essential for motility, invasion and replication. The IMC subcompartment proteins (ISP) have recently been identified inToxoplasma gondiiand shown to be critical for replication, although their specific mechanisms are unknown. Structural characterization ofTgISP1 was pursued in order to identify the fold adopted by the ISPs and to generate detailed insight into how this family of proteins functions during replication. An N-terminally truncated form ofTgISP1 was purified fromEscherichia coli, crystallized and subjected to X-ray diffraction analysis. Two crystal forms ofTgISP1 belonging to space groupsP4132 orP4332 andP212121diffracted to 2.05 and 2.1 Å resolution, respectively.
Print ISSN:
1744-3091
Topics:
Biology
,
Chemistry and Pharmacology
,
Geosciences
,
Physics
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