6wti | pdb_00006wti
The Cryo-EM structure of the ubiquinol oxidase from Escherichia coli
Structural highlights
FunctionCYOB_ECOLI Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron. Protons are probably pumped via D- and K- channels found in this subunit (PubMed:11017202).[1] [2] [3] Publication Abstract from PubMedSingle-particle cryo-electron microscopy (cryo-EM) has become a powerful technique in the field of structural biology. However, the inability to reliably produce pure, homogeneous membrane protein samples hampers the progress of their structural determination. Here, we develop a bottom-up iterative method, Build and Retrieve (BaR), that enables the identification and determination of cryo-EM structures of a variety of inner and outer membrane proteins, including membrane protein complexes of different sizes and dimensions, from a heterogeneous, impure protein sample. We also use the BaR methodology to elucidate structural information from Escherichia coli K12 crude membrane and raw lysate. The findings demonstrate that it is possible to solve high-resolution structures of a number of relatively small (<100 kDa) and less abundant (<10%) unidentified membrane proteins within a single, heterogeneous sample. Importantly, these results highlight the potential of cryo-EM for systems structural proteomics. A 'Build and Retrieve' methodology to simultaneously solve cryo-EM structures of membrane proteins.,Su CC, Lyu M, Morgan CE, Bolla JR, Robinson CV, Yu EW Nat Methods. 2021 Jan;18(1):69-75. doi: 10.1038/s41592-020-01021-2. Epub 2021 Jan, 6. PMID:33408407[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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