5l0y | pdb_00005l0y

Crystal Structure of a Sec72-ssa1 c-terminal peptide fusion protein

spinqualitylabelsall models 5l0y, resolution 2.87Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5l0y is a 13 chain structure with sequence from Chaetomium thermophilum, Chaetomium thermophilum var. thermophilum DSM 1495 and Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.87Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0RYP6_CHATD G0SH41_CHATD Publication Abstract from PubMed The biosynthesis of many eukaryotic proteins requires accurate targeting to and translocation across the endoplasmic reticulum (ER) membrane. Post-translational protein translocation in yeast requires both the Sec61 translocation channel, and a complex of four additional proteins: Sec63, Sec62, Sec71, and Sec72. The structure and function of these proteins are largely unknown. This pathway also requires the cytosolic Hsp70 protein Ssa1, but whether Ssa1 associates with the translocation machinery to target protein substrates to the membrane is unclear. Here, we use a combined structural and biochemical approach to explore the role of Sec71/Sec72 subcomplex in post-translational protein translocation. To this end, we report a crystal structure of the Sec71/Sec72 complex, which revealed that Sec72 contains a tetratricopeptide repeat (TPR) domain that is anchored to the ER membrane by Sec71. We also determined the crystal structure of this TPR domain with a C-terminal peptide derived from Ssa1, which suggests how Sec72 interacts with full-length Ssa1. Surprisingly, Ssb1, a cytoplasmic Hsp70 that binds ribosome- associated nascent polypeptide chains also binds to the TPR domain of Sec72, even though it lacks the TPR-binding C-terminal residues of Ssa1. We demonstrate that Ssb1 binds through its ATPase domain to the TPR domain, an interaction that leads to inhibition of nucleotide exchange. Taken together, our results suggest that translocation substrates can be recruited to the Sec71/72 complex either post-translationally through Ssa1 or co-translationally through Ssb1. Two alternative binding mechanisms connect the protein translocation Sec71/Sec72 complex with heat shock proteins.,Tripathi A, Mandon EC, Gilmore R, Rapoport TA J Biol Chem. 2017 Mar 12. pii: jbc.M116.761122. doi: 10.1074/jbc.M116.761122. PMID:28286332 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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