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Instruments / Technical Area	Publication Details	Published
Krios I-Titan Krios I at Diamond	Mechanism of membrane-tethered mitochondrial protein synthesis Yuzuru Itoh , Juni Andrell , Austin Choi , Uwe Richter , Priyanka Maiti , Robert B. Best , Antoni Barrientos , Brendan J. Battersby , Alexey Amunts Science 371, 846 - 849 DOI: 10.1126/science.abe0763 Diamond Proposal Number(s): [19823] Show Abstract ▼ Abstract: Mitochondrial ribosomes (mitoribosomes) are tethered to the mitochondrial inner membrane to facilitate the cotranslational membrane insertion of the synthesized proteins. We report cryo–electron microscopy structures of human mitoribosomes with nascent polypeptide, bound to the insertase oxidase assembly 1–like (OXA1L) through three distinct contact sites. OXA1L binding is correlated with a series of conformational changes in the mitoribosomal large subunit that catalyze the delivery of newly synthesized polypeptides. The mechanism relies on the folding of mL45 inside the exit tunnel, forming two specific constriction sites that would limit helix formation of the nascent chain. A gap is formed between the exit and the membrane, making the newly synthesized proteins accessible. Our data elucidate the basis by which mitoribosomes interact with the OXA1L insertase to couple protein synthesis and membrane delivery.	Feb 2021
Krios II-Titan Krios II at Diamond	Structure of the chloroplast ribosome with chl-RRF and hibernation-promoting factor Annemarie Perez Boerema , Shintaro Aibara , Bijoya Paul , Victor Tobiasson , Dari Kimanius , Björn O. Forsberg , Karin Wallden , Erik Lindahl , Alexey Amunts Nature Plants 4, 212 - 217 DOI: 10.1038/s41477-018-0129-6 Diamond Proposal Number(s): [15290] Show Abstract ▼ Abstract: Oxygenic photosynthesis produces oxygen and builds a variety of organic compounds, changing the chemistry of the air, the sea and fuelling the food chain on our planet. The photochemical reactions underpinning this process in plants take place in the chloroplast. Chloroplasts evolved ~1.2 billion years ago from an engulfed primordial diazotrophic cyanobacterium, and chlororibosomes are responsible for synthesis of the core proteins driving photochemical reactions. Chlororibosomal activity is spatiotemporally coupled to the synthesis and incorporation of functionally essential co-factors, implying the presence of chloroplast-specific regulatory mechanisms and structural adaptation of the chlororibosome1,2. Despite recent structural information3,4,5,6, some of these aspects remained elusive. To provide new insights into the structural specialities and evolution, we report a comprehensive analysis of the 2.9–3.1 Å resolution electron cryo-microscopy structure of the spinach chlororibosome in complex with its recycling factor and hibernation-promoting factor. The model reveals a prominent channel extending from the exit tunnel to the chlororibosome exterior, structural re-arrangements that lead to increased surface area for translocon binding, and experimental evidence for parallel and convergent evolution of chloro- and mitoribosomes.	Apr 2018
I04-Macromolecular Crystallography	Bactobolin A Binds to a Site on the 70S Ribosome Distinct from Previously Seen Antibiotics Alexey Amunts , Karol Fiedorczuk , Thao T. Truong , Josephine Chandler , E. Peter Greenberg , V. Ramakrishnan Journal Of Molecular Biology 427 (4), 753 - 755 DOI: 10.1016/j.jmb.2014.12.018 PMID: 25562208 Open Access Show Abstract ▼ Abstract: The ribosome is the target of a large number of antibiotics. Here, we report a 3.4-Å-resolution crystal structure of bactobolin A bound to 70S ribosome–tRNA complex. The antibiotic binds at a previously unseen site in the 50S subunit and displaces tRNA bound at the P-site. It thus likely has a similar mechanism of action as blasticidin S despite binding to a different site. The structure also rationalizes previously identified resistance mutations.	Feb 2015

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