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Title:
Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria - PubMed
Description:
In the crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 A resolution, the three catalytic beta-subunits differ in conformation and in the bound nucleotide. The structure supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different …
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Keywords {🔍}
doi, pmid, structure, fatpase, catalytic, pmc, protein, free, article, articles, cited, bovine, leslie, walker, atpases, main, states, ncbi, abstract, similar, mesh, resources, nature, aug, resolution, conformation, atp, synthase, pubmed, biol, sci, review, epub, molecular, protontranslocating, hhs, page, content, homepage, navigation, search, full, text, comment, publication, types, terms, substances, related, information,
Topics {✒️}
vacuolar-type atpases main page content literature sources rna-dependent hexameric helicase similar articles cited regulatory protein if1 resources nature catalytic beta-subunits differ x-ray structure determination conformation alpha-helical domain x-ray mitochondria rotary catalysis bovine f1-atpase intact atp synthase bovine heart mitochondria carboxy-terminal region sotelo-mundo rr cryo-em studies mazhab-jafari mt nat struct biol torque transmission mechanism gamma-subunit arch biochem biophys cited united states government 1038/370621a0 abstract f1-atpase f1-atpase] atp synthase bound nucleotide abstract catalytic subunits biol sci structural importance hhs catalytic mechanism sci adv walker je crystal structure structure supports enzyme structure pubmed wordmark pubmed logo catalytic cycle catalytic centers official website primary source cross rl philos trans
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