4xzv
From Proteopedia
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| - | ''' | + | ==Crystal Structure of SLMO1-TRIAP1 Complex== |
| + | <StructureSection load='4xzv' size='340' side='right' caption='[[4xzv]], [[Resolution|resolution]] 3.58Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4xzv]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XZV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XZV 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> | ||
| + | <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=4xzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xzv OCA], [http://pdbe.org/4xzv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xzv RCSB], [http://www.ebi.ac.uk/pdbsum/4xzv PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:26071602</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 4xzv" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Garnett, J A]] | ||
| + | [[Category: Matthews, S J]] | ||
[[Category: Miliara, X]] | [[Category: Miliara, X]] | ||
| + | [[Category: Apoptosis]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Lipid transport]] | ||
| + | [[Category: Mitochondria]] | ||
Revision as of 17:07, 20 January 2016
Crystal Structure of SLMO1-TRIAP1 Complex
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