8dmf: Difference between revisions
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==Cryo-EM structure of the ribosome-bound Bacteroides thetaiotaomicron EF-G2== | |||
<StructureSection load='8dmf' size='340' side='right'caption='[[8dmf]], [[Resolution|resolution]] 4.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8dmf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron_VPI-5482 Bacteroides thetaiotaomicron VPI-5482]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DMF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8dmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dmf OCA], [https://pdbe.org/8dmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dmf RCSB], [https://www.ebi.ac.uk/pdbsum/8dmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dmf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8A5S1_BACTN Q8A5S1_BACTN] Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.[ARBA:ARBA00003987] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:36472247</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8dmf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacteroides thetaiotaomicron VPI-5482]] | |||
[[Category: Large Structures]] | |||
[[Category: Groisman EA]] | |||
[[Category: Han W]] | |||
[[Category: Liu J]] | |||
[[Category: Wang C]] | |||
