6bxt

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of Toxoplasma gondii Mitochondrial Association Factor 1 A (MAF1A) in complex with ADPribose

Structural highlights

6bxt is a 3 chain structure with sequence from Toxoplasma gondii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.7Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3]

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Adomako-Ankomah Y, English ED, Danielson JJ, Pernas LF, Parker ML, Boulanger MJ, Dubey JP, Boyle JP. Host Mitochondrial Association Evolved in the Human Parasite Toxoplasma gondii via Neofunctionalization of a Gene Duplicate. Genetics. 2016 May;203(1):283-98. PMID:26920761 doi:10.1534/genetics.115.186270
↑ Blank ML, Parker ML, Ramaswamy R, Powell CJ, English ED, Adomako-Ankomah Y, Pernas LF, Workman SD, Boothroyd JC, Boulanger MJ, Boyle JP. A Toxoplasma gondii locus required for the direct manipulation of host mitochondria has maintained multiple ancestral functions. Mol Microbiol. 2018 Jun;108(5):519-535. doi: 10.1111/mmi.13947. Epub 2018 Apr 11. PMID:29505111 doi:http://dx.doi.org/10.1111/mmi.13947
↑ Blank ML, Xia J, Morcos MM, Sun M, Cantrell PS, Liu Y, Zeng X, Powell CJ, Yates N, Boulanger MJ, Boyle JP. Toxoplasma gondii association with host mitochondria requires key mitochondrial protein import machinery. Proc Natl Acad Sci U S A. 2021 Mar 23;118(12):e2013336118. PMID:33723040 doi:10.1073/pnas.2013336118
↑ Blank ML, Parker ML, Ramaswamy R, Powell CJ, English ED, Adomako-Ankomah Y, Pernas LF, Workman SD, Boothroyd JC, Boulanger MJ, Boyle JP. A Toxoplasma gondii locus required for the direct manipulation of host mitochondria has maintained multiple ancestral functions. Mol Microbiol. 2018 Jun;108(5):519-535. doi: 10.1111/mmi.13947. Epub 2018 Apr 11. PMID:29505111 doi:http://dx.doi.org/10.1111/mmi.13947

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6bxt"

Categories: Large Structures | Toxoplasma gondii | Boulanger MJ | Parker ML | Ramaswamy R

@@ Line 1: / Line 1: @@
 ==Crystal structure of Toxoplasma gondii Mitochondrial Association Factor 1 A (MAF1A) in complex with ADPribose==
-<StructureSection load='6bxt' size='340' side='right' caption='[[6bxt]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='6bxt' size='340' side='right'caption='[[6bxt]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6bxt]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxgo Toxgo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BXT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BXT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6bxt]] 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=6BXT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BXT FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6bxs|6bxs]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5811 TOXGO])</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=6bxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bxt OCA], [https://pdbe.org/6bxt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bxt RCSB], [https://www.ebi.ac.uk/pdbsum/6bxt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bxt ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6bxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bxt OCA], [http://pdbe.org/6bxt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bxt RCSB], [http://www.ebi.ac.uk/pdbsum/6bxt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bxt 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 ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Toxgo]]
+[[Category: Large Structures]]
-[[Category: Boulanger, M J]]
+[[Category: Toxoplasma gondii]]
-[[Category: Parker, M L]]
+[[Category: Boulanger MJ]]
-[[Category: Ramaswamy, R]]
+[[Category: Parker ML]]
-[[Category: Adpribose]]
+[[Category: Ramaswamy R]]
-[[Category: Macro domain]]
-[[Category: Membrane protein]]
-[[Category: Neofunctionalize]]

6bxt

From Proteopedia

Current revision

Crystal structure of Toxoplasma gondii Mitochondrial Association Factor 1 A (MAF1A) in complex with ADPribose

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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