5C8J
A YidC-like protein in the archaeal plasma membrane
Summary for 5C8J
| Entry DOI | 10.2210/pdb5c8j/pdb |
| Descriptor | Antibody fragment, heavy chain, Antibody fragment, light chain, Protein MJ0480, ... (4 entities in total) |
| Functional Keywords | membrane protein insertase, membrane protein |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 12 |
| Total formula weight | 292699.79 |
| Authors | Borowska, M.T.,Dominik, P.K.,Anghel, S.A.,Kossiakoff, A.A.,Keenan, R.J. (deposition date: 2015-06-25, release date: 2015-09-02, Last modification date: 2024-10-09) |
| Primary citation | Borowska, M.T.,Dominik, P.K.,Anghel, S.A.,Kossiakoff, A.A.,Keenan, R.J. A YidC-like Protein in the Archaeal Plasma Membrane. Structure, 23:1715-1724, 2015 Cited by PubMed Abstract: Cells possess specialized machinery to direct the insertion of membrane proteins into the lipid bilayer. In bacteria, the essential protein YidC inserts certain proteins into the plasma membrane, and eukaryotic orthologs are present in the mitochondrial inner membrane and the chloroplast thylakoid membrane. The existence of homologous insertases in archaea has been proposed based on phylogenetic analysis. However, limited sequence identity, distinct architecture, and the absence of experimental data have made this assignment ambiguous. Here we describe the 3.5-Å crystal structure of an archaeal DUF106 protein from Methanocaldococcus jannaschii (Mj0480), revealing a lipid-exposed hydrophilic surface presented by a conserved YidC-like fold. Functional analysis reveals selective binding of Mj0480 to ribosomes displaying a stalled YidC substrate, and a direct interaction between the buried hydrophilic surface of Mj0480 and the nascent chain. These data provide direct experimental evidence that the archaeal DUF106 proteins are YidC/Oxa1/Alb3-like insertases of the archaeal plasma membrane. PubMed: 26256539DOI: 10.1016/j.str.2015.06.025 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.502 Å) |
Structure validation
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