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| | <StructureSection load='4xzs' size='340' side='right'caption='[[4xzs]], [[Resolution|resolution]] 2.12Å' scene=''> | | <StructureSection load='4xzs' size='340' side='right'caption='[[4xzs]], [[Resolution|resolution]] 2.12Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xzs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XZS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XZS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xzs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XZS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XZS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRIAP1, 15E1.1, HSPC132 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4xzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xzs OCA], [https://pdbe.org/4xzs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xzs RCSB], [https://www.ebi.ac.uk/pdbsum/4xzs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xzs 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=4xzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xzs OCA], [http://pdbe.org/4xzs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xzs RCSB], [http://www.ebi.ac.uk/pdbsum/4xzs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xzs ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. | + | [https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/TRIA1_HUMAN TRIA1_HUMAN] Involved in the modulation of the mitochondrial apoptotic pathway by ensuring the accumulation of cardiolipin (CL) in mitochondrial membranes. In vitro, the TRIAP1:PRELID1 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space to provide PA for CL synthesis in the inner membrane (PubMed:23931759). Likewise, the TRIAP1:PRELID3A complex mediates the transfer of phosphatidic acid (PA) between liposomes (in vitro) and probably functions as a PA transporter across the mitochondrion intermembrane space (in vivo) (PubMed:26071602). Mediates cell survival by inhibiting activation of caspase-9 which prevents induction of apoptosis (PubMed:15735003).<ref>PMID:15735003</ref> <ref>PMID:23931759</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Escherichia coli K-12]] |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Abid-Ali, F]] | + | [[Category: Abid-Ali F]] |
| - | [[Category: Garnett, J A]] | + | [[Category: Garnett JA]] |
| - | [[Category: Matthews, S J]] | + | [[Category: Matthews SJ]] |
| - | [[Category: Miliara, X]] | + | [[Category: Miliara X]] |
| - | [[Category: Perez-Dorado, I]] | + | [[Category: Perez-Dorado I]] |
| - | [[Category: Apoptosis]]
| + | |
| - | [[Category: Cancer]]
| + | |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Cx9cx motif]]
| + | |
| - | [[Category: Lipid]]
| + | |
| - | [[Category: Mitochondria]]
| + | |
| Structural highlights
Function
MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.TRIA1_HUMAN Involved in the modulation of the mitochondrial apoptotic pathway by ensuring the accumulation of cardiolipin (CL) in mitochondrial membranes. In vitro, the TRIAP1:PRELID1 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space to provide PA for CL synthesis in the inner membrane (PubMed:23931759). Likewise, the TRIAP1:PRELID3A complex mediates the transfer of phosphatidic acid (PA) between liposomes (in vitro) and probably functions as a PA transporter across the mitochondrion intermembrane space (in vivo) (PubMed:26071602). Mediates cell survival by inhibiting activation of caspase-9 which prevents induction of apoptosis (PubMed:15735003).[1] [2]
Publication Abstract from PubMed
The composition of the mitochondrial membrane is important for its architecture and proper function. Mitochondria depend on a tightly regulated supply of phospholipid via intra-mitochondrial synthesis and by direct import from the endoplasmic reticulum. The Ups1/PRELI-like family together with its mitochondrial chaperones (TRIAP1/Mdm35) represent a unique heterodimeric lipid transfer system that is evolutionary conserved from yeast to man. Work presented here provides new atomic resolution insight into the function of a human member of this system. Crystal structures of free TRIAP1 and the TRIAP1-SLMO1 complex reveal how the PRELI domain is chaperoned during import into the intermembrane mitochondrial space. The structural resemblance of PRELI-like domain of SLMO1 with that of mammalian phoshatidylinositol transfer proteins (PITPs) suggest that they share similar lipid transfer mechanisms, in which access to a buried phospholipid-binding cavity is regulated by conformationally adaptable loops.
Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes.,Miliara X, Garnett JA, Tatsuta T, Abid Ali F, Baldie H, Perez-Dorado I, Simpson P, Yague E, Langer T, Matthews S EMBO Rep. 2015 Jul;16(7):824-35. doi: 10.15252/embr.201540229. Epub 2015 Jun 12. PMID:26071602[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Park WR, Nakamura Y. p53CSV, a novel p53-inducible gene involved in the p53-dependent cell-survival pathway. Cancer Res. 2005 Feb 15;65(4):1197-206. PMID:15735003 doi:http://dx.doi.org/65/4/1197
- ↑ Potting C, Tatsuta T, Konig T, Haag M, Wai T, Aaltonen MJ, Langer T. TRIAP1/PRELI complexes prevent apoptosis by mediating intramitochondrial transport of phosphatidic acid. Cell Metab. 2013 Aug 6;18(2):287-95. doi: 10.1016/j.cmet.2013.07.008. PMID:23931759 doi:http://dx.doi.org/10.1016/j.cmet.2013.07.008
- ↑ Miliara X, Garnett JA, Tatsuta T, Abid Ali F, Baldie H, Perez-Dorado I, Simpson P, Yague E, Langer T, Matthews S. Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes. EMBO Rep. 2015 Jul;16(7):824-35. doi: 10.15252/embr.201540229. Epub 2015 Jun 12. PMID:26071602 doi:http://dx.doi.org/10.15252/embr.201540229
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