6cp9
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6cp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cp9 OCA], [http://pdbe.org/6cp9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cp9 RCSB], [http://www.ebi.ac.uk/pdbsum/6cp9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cp9 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6cp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cp9 OCA], [http://pdbe.org/6cp9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cp9 RCSB], [http://www.ebi.ac.uk/pdbsum/6cp9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cp9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Contact-dependent growth inhibition (CDI) is a form of interbacterial competition mediated by CdiB-CdiA two-partner secretion systems. CdiA effector proteins carry polymorphic C-terminal toxin domains (CdiA-CT), which are neutralized by specific CdiI immunity proteins to prevent self-inhibition. Here, we present the crystal structures of CdiA-CTCdiI complexes from Klebsiella pneumoniae 342 and Escherichia coli 3006. The toxins adopt related folds that resemble the ribonuclease domain of colicin D, and both are isoacceptor-specific tRNases that cleave the acceptor stem of deacylated tRNAGAU(Ile). Although the toxins are similar in structure and substrate specificity, CdiA-CT(Kp342) activity requires translation factors EF-Tu and EF-Ts, whereas CdiA-CT(EC3006) is intrinsically active. Furthermore, the corresponding immunity proteins are unrelated in sequence and structure. CdiI(Kp342) forms a dimeric beta sandwich, whereas CdiI(EC3006) is an alpha-solenoid monomer. Given that toxin-immunity genes co-evolve as linked pairs, these observations suggest that the similarities in toxin structure and activity reflect functional convergence. | ||
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| + | Convergent Evolution of the Barnase/EndoU/Colicin/RelE (BECR) Fold in Antibacterial tRNase Toxins.,Gucinski GC, Michalska K, Garza-Sanchez F, Eschenfeldt WH, Stols L, Nguyen JY, Goulding CW, Joachimiak A, Hayes CS Structure. 2019 Sep 6. pii: S0969-2126(19)30281-3. doi:, 10.1016/j.str.2019.08.010. PMID:31515004<ref>PMID:31515004</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6cp9" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Contact-dependent growth inhibition toxin - immunity protein complex from Klebsiella pneumoniae 342
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Categories: Klep3 | Large Structures | Eschenfeldt, W | Goulding, C W | Hayes, C S | Joachimiak, A | Structural genomic | Michalska, K | Stols, L | UC4CDI, Structure-Function Analysis of Polymorphic CDI Toxin-Immunity Protein Complexes | Mcsg | PSI, Protein structure initiative | Psi-biology | Rnase | Structure-function analysis of polymorphic cdi toxin-immunity protein complex | Toxin | Toxin-antitoxin complex | Uc4cdi
