View source for 6bxs


==Crystal structure of Toxoplasma gondii Mitochondrial Association Factor 1 A (MAF1A)==
<StructureSection load='6bxs' size='340' side='right'caption='[[6bxs]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6bxs]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BXS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BXS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6bxs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bxs OCA], [https://pdbe.org/6bxs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bxs RCSB], [https://www.ebi.ac.uk/pdbsum/6bxs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bxs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MAFA1_TOXGO MAFA1_TOXGO] During host cell infection by tachyzoites, does not play a role in tethering the parasitophorous vacuole to the host mitochondria, probably because it does not bind host mitochondrial import protein TOMM70.<ref>PMID:26920761</ref> <ref>PMID:29505111</ref> <ref>PMID:33723040</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Toxoplasma gondii locus mitochondrial association factor 1 (MAF1) encodes multiple paralogs, some of which mediate host mitochondrial association (HMA). Previous work showed that HMA was a trait that arose in T. gondii through neofunctionalization of an ancestral MAF1 ortholog. Structural analysis of HMA-competent and incompetent MAF1 paralogs (MAF1b and MAF1a, respectively) revealed that both paralogs harbor an ADP ribose binding macro-domain, with comparatively low (micromolar) affinity for ADP ribose. Replacing the 16 C-terminal residues of MAF1b with those of MAF1a abrogated HMA, and we also show that only three residues in the C-terminal helix are required for MAF1-mediated HMA. Importantly these same three residues are also required for the in vivo growth advantage conferred by MAF1b, providing a definitive link between in vivo proliferation and manipulation of host mitochondria. Co-immunoprecipitation assays reveal that the ability to interact with the mitochondrial MICOS complex is shared by HMA-competent and incompetent MAF1 paralogs and mutants. The weak ADPr coordination and ability to interact with the MICOS complex shared between divergent paralogs may represent modular ancestral functions for this tandemly expanded and diversified T. gondii locus.

A Toxoplasma gondii locus required for the direct manipulation of host mitochondria has maintained multiple ancestral functions.,Blank ML, Parker ML, Ramaswamy R, Powell CJ, English ED, Adomako-Ankomah Y, Pernas LF, Workman SD, Boothroyd JC, Boulanger MJ, Boyle JP Mol Microbiol. 2018 Jun;108(5):519-535. doi: 10.1111/mmi.13947. Epub 2018 Apr 11. PMID:29505111<ref>PMID:29505111</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6bxs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Toxoplasma gondii]]
[[Category: Boulanger MJ]]
[[Category: Ramaswamy R]]