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http://purl.uniprot.org/citations/26071601http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26071601http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26071601http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.org/dc/terms/identifier"doi:10.15252/embr.201540137"xsd:string
http://purl.uniprot.org/citations/26071601http://purl.org/dc/terms/identifier"doi:10.15252/embr.201540137"xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"Ding J."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"Ding J."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"He F."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"He F."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"Li J."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"Li J."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"Wang C."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"Wang C."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"Yao H."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"Yao H."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"Wang J."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"Wang J."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"Zhang P."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"Zhang P."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"Xue H."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"Xue H."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"Qi X."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"Qi X."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"Yu F."xsd:string
http://purl.uniprot.org/citations/26071601http://purl.uniprot.org/core/author"Yu F."xsd:string