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Structure of human mitochondrial trifunctional protein, octamerStructure of human mitochondrial trifunctional protein, octamer
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Structural highlights
Disease[ECHA_HUMAN] Mitochondrial trifunctional protein deficiency;Acute fatty liver of pregnancy;Long chain 3-hydroxyacyl-CoA dehydrogenase deficiency. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. [ECHB_HUMAN] Mitochondrial trifunctional protein deficiency. The disease is caused by mutations affecting the gene represented in this entry. Function[ECHA_HUMAN] Bifunctional subunit. Publication Abstract from PubMedThe mitochondrial trifunctional protein (TFP) catalyzes three reactions in the fatty acid beta-oxidation process. Mutations in the two TFP subunits cause mitochondrial trifunctional protein deficiency and acute fatty liver of pregnancy that can lead to death. Here we report a 4.2-A cryo-electron microscopy alpha2beta2 tetrameric structure of the human TFP. The tetramer has a V-shaped architecture that displays a distinct assembly compared with the bacterial TFPs. A concave surface of the TFP tetramer interacts with the detergent molecules in the structure, suggesting that this region is involved in associating with the membrane. Deletion of a helical hairpin in TFPbeta decreases its binding to the liposomes in vitro and reduces its membrane targeting in cells. Our results provide the structural basis for TFP function and have important implications for fatty acid oxidation related diseases. Cryo-EM structure of human mitochondrial trifunctional protein.,Liang K, Li N, Wang X, Dai J, Liu P, Wang C, Chen XW, Gao N, Xiao J Proc Natl Acad Sci U S A. 2018 Jun 18. pii: 1801252115. doi:, 10.1073/pnas.1801252115. PMID:29915090[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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