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| | <StructureSection load='6cp8' size='340' side='right'caption='[[6cp8]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='6cp8' size='340' side='right'caption='[[6cp8]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6cp8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CP8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CP8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6cp8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CP8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.201Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BTQ06_14245 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), BTQ06_14240 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=6cp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cp8 OCA], [https://pdbe.org/6cp8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cp8 RCSB], [https://www.ebi.ac.uk/pdbsum/6cp8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cp8 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=6cp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cp8 OCA], [http://pdbe.org/6cp8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cp8 RCSB], [http://www.ebi.ac.uk/pdbsum/6cp8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cp8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A2A2CAY5_ECOLX A0A2A2CAY5_ECOLX] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Eschenfeldt, W]] | + | [[Category: Eschenfeldt W]] |
| - | [[Category: Goulding, C W]] | + | [[Category: Goulding CW]] |
| - | [[Category: Hayes, C S]] | + | [[Category: Hayes CS]] |
| - | [[Category: Joachimiak, A]] | + | [[Category: Joachimiak A]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Michalska K]] |
| - | [[Category: Michalska, K]] | + | [[Category: Stols L]] |
| - | [[Category: Stols, L]] | + | |
| - | [[Category: UC4CDI, Structure-Function Analysis of Polymorphic CDI Toxin-Immunity Protein Complexes]]
| + | |
| - | [[Category: Mcsg]]
| + | |
| - | [[Category: Psi-biology]]
| + | |
| - | [[Category: Rnase]]
| + | |
| - | [[Category: Structure-function analysis of polymorphic cdi toxin-immunity protein complex]]
| + | |
| - | [[Category: Toxin]]
| + | |
| - | [[Category: Toxin-antitoxin complex]]
| + | |
| - | [[Category: Uc4cdi]]
| + | |
| Structural highlights
Function
A0A2A2CAY5_ECOLX
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gucinski GC, Michalska K, Garza-Sanchez F, Eschenfeldt WH, Stols L, Nguyen JY, Goulding CW, Joachimiak A, Hayes CS. Convergent Evolution of the Barnase/EndoU/Colicin/RelE (BECR) Fold in Antibacterial tRNase Toxins. Structure. 2019 Sep 6. pii: S0969-2126(19)30281-3. doi:, 10.1016/j.str.2019.08.010. PMID:31515004 doi:http://dx.doi.org/10.1016/j.str.2019.08.010
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