4XIZ
Structure of a phospholipid trafficking complex with substrate
Summary for 4XIZ
| Entry DOI | 10.2210/pdb4xiz/pdb |
| Related | 4XHR |
| Descriptor | Protein UPS1, mitochondrial, Mitochondrial distribution and morphology protein 35, 2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE, ... (4 entities in total) |
| Functional Keywords | phospholipid, lipid transport-oxidoreductase complex, lipid transport/oxidoreductase |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Cellular location | Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side: Q05776 Cytoplasm: O60200 |
| Total number of polymer chains | 4 |
| Total formula weight | 56236.09 |
| Authors | |
| Primary citation | Yu, F.,He, F.,Yao, H.,Wang, C.,Wang, J.,Li, J.,Qi, X.,Xue, H.,Ding, J.,Zhang, P. Structural basis of intramitochondrial phosphatidic acid transport mediated by Ups1-Mdm35 complex Embo Rep., 16:813-823, 2015 Cited by PubMed Abstract: Ups1 forms a complex with Mdm35 and is critical for the transport of phosphatidic acid (PA) from the mitochondrial outer membrane to the inner membrane. We report the crystal structure of the Ups1-Mdm35-PA complex and the functional characterization of Ups1-Mdm35 in PA binding and transfer. Ups1 features a barrel-like structure consisting of an antiparallel β-sheet and three α-helices. Mdm35 adopts a three-helical clamp-like structure to wrap around Ups1 to form a stable complex. The β-sheet and α-helices of Ups1 form a long tunnel-like pocket to accommodate the substrate PA, and a short helix α2 acts as a lid to cover the pocket. The hydrophobic residues lining the pocket and helix α2 are critical for PA binding and transfer. In addition, a hydrophilic patch on the surface of Ups1 near the PA phosphate-binding site also plays an important role in the function of Ups1-Mdm35. Our study reveals the molecular basis of the function of Ups1-Mdm35 and sheds new light on the mechanism of intramitochondrial phospholipid transport by the MSF1/PRELI family proteins. PubMed: 26071601DOI: 10.15252/embr.201540137 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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