8dmf

Cryo-EM structure of the ribosome-bound Bacteroides thetaiotaomicron EF-G2

spinqualitylabelsall models 8dmf, resolution 4.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8dmf is a 1 chain structure with sequence from Bacteroides thetaiotaomicron VPI-5482. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 4Å Ligands: GTP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8A5S1_BACTN Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.[ARBA:ARBA00003987] Publication Abstract from PubMed Protein synthesis is crucial for cell growth and survival yet one of the most energy-consuming cellular processes. How, then, do cells sustain protein synthesis under starvation conditions when energy is limited? To accelerate the translocation of mRNA-tRNAs through the ribosome, bacterial elongation factor G (EF-G) hydrolyzes energy-rich guanosine triphosphate (GTP) for every amino acid incorporated into a protein. Here, we identify an EF-G paralog-EF-G2-that supports translocation without hydrolyzing GTP in the gut commensal bacterium Bacteroides thetaiotaomicron. EF-G2's singular ability to sustain protein synthesis, albeit at slow rates, is crucial for bacterial gut colonization. EF-G2 is ~10-fold more abundant than canonical EF-G1 in bacteria harvested from murine ceca and, unlike EF-G1, specifically accumulates during carbon starvation. Moreover, we uncover a 26-residue region unique to EF-G2 that is essential for protein synthesis, EF-G2 dissociation from the ribosome, and responsible for the absence of GTPase activity. Our findings reveal how cells curb energy consumption while maintaining protein synthesis to advance fitness in nutrient-fluctuating environments. Gut colonization by Bacteroides requires translation by an EF-G paralog lacking GTPase activity.,Han W, Peng BZ, Wang C, Townsend GE 2nd, Barry NA, Peske F, Goodman AL, Liu J, Rodnina MV, Groisman EA EMBO J. 2023 Jan 16;42(2):e112372. doi: 10.15252/embj.2022112372. Epub 2022 Dec , 6. PMID:36472247 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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