4XZV
Crystal Structure of SLMO1-TRIAP1 Complex
Summary for 4XZV
| Entry DOI | 10.2210/pdb4xzv/pdb |
| Related PRD ID | PRD_900001 |
| Descriptor | Maltose-binding periplasmic protein,TP53-regulated inhibitor of apoptosis 1, Protein slowmo homolog 1, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total) |
| Functional Keywords | apoptosis, lipid transport, mitochondria, complex |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 8 |
| Total formula weight | 281086.39 |
| Authors | Miliara, X.,Garnett, J.A.,Matthews, S.J. (deposition date: 2015-02-05, release date: 2016-01-20, Last modification date: 2024-11-06) |
| Primary citation | Miliara, X.,Garnett, J.A.,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., 16:824-835, 2015 Cited by PubMed Abstract: 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. PubMed: 26071602DOI: 10.15252/embr.201540229 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.58 Å) |
Structure validation
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