View source for 7vmc


==Crystal structure of EF-Tu/CdiA/CdiI==
<StructureSection load='7vmc' size='340' side='right'caption='[[7vmc]], [[Resolution|resolution]] 3.41&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7vmc]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7_str._EC869 Escherichia coli O157:H7 str. EC869]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VMC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.413&#8491;</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=7vmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vmc OCA], [https://pdbe.org/7vmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vmc RCSB], [https://www.ebi.ac.uk/pdbsum/7vmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vmc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EFTU2_ECOLI EFTU2_ECOLI] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118]  May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.[HAMAP-Rule:MF_00118]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Contact-dependent growth inhibition is a mechanism of interbacterial competition mediated by delivery of the C-terminal toxin domain of CdiA protein (CdiA-CT) into neighboring bacteria. The CdiA-CT of enterohemorrhagic Escherichia coli EC869 (CdiA-CTEC869) cleaves the 3'-acceptor regions of specific tRNAs in a reaction that requires the translation factors Tu/Ts and GTP. Here, we show that CdiA-CTEC869 has an intrinsic ability to recognize a specific sequence in substrate tRNAs, and Tu:Ts complex promotes tRNA cleavage by CdiA-CTEC869. Uncharged and aminoacylated tRNAs (aa-tRNAs) were cleaved by CdiA-CTEC869 to the same extent in the presence of Tu/Ts, and the CdiA-CTEC869:Tu:Ts:tRNA(aa-tRNA) complex formed in the presence of GTP. CdiA-CTEC869 interacts with domain II of Tu, thereby preventing the 3'-moiety of tRNA to bind to Tu as in canonical Tu:GTP:aa-tRNA complexes. Superimposition of the Tu:GTP:aa-tRNA structure onto the CdiA-CTEC869:Tu structure suggests that the 3'-portion of tRNA relocates into the CdiA-CTEC869 active site, located on the opposite side to the CdiA-CTEC869 :Tu interface, for tRNA cleavage. Thus, CdiA-CTEC869 is recruited to Tu:GTP:Ts, and CdiA-CT:Tu:GTP:Ts recognizes substrate tRNAs and cleaves them. Tu:GTP:Ts serves as a reaction scaffold that increases the affinity of CdiA-CTEC869 for substrate tRNAs and induces a structural change of tRNAs for efficient cleavage by CdiA-CTEC869.

Mechanistic insights into tRNA cleavage by a contact-dependent growth inhibitor protein and translation factors.,Wang J, Yashiro Y, Sakaguchi Y, Suzuki T, Tomita K Nucleic Acids Res. 2022 May 6;50(8):4713-4731. doi: 10.1093/nar/gkac228. PMID:35411396<ref>PMID:35411396</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7vmc" style="background-color:#fffaf0;"></div>

==See Also==
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli O157:H7 str. EC869]]
[[Category: Large Structures]]
[[Category: Tomita K]]
[[Category: Wang J]]
[[Category: Yashiro Y]]