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| | <StructureSection load='4ml0' size='340' side='right'caption='[[4ml0]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='4ml0' size='340' side='right'caption='[[4ml0]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ml0]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecobr Ecobr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ML0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ML0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ml0]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_B_str._REL606 Escherichia coli B str. REL606]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ML0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ML0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ml2|4ml2]], [[4mmg|4mmg]], [[4mmj|4mmj]]</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=4ml0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ml0 OCA], [https://pdbe.org/4ml0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ml0 RCSB], [https://www.ebi.ac.uk/pdbsum/4ml0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ml0 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dinJ, ECB_00221 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=413997 ECOBR]), yafQ, ECB_00220 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=413997 ECOBR])</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=4ml0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ml0 OCA], [http://pdbe.org/4ml0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ml0 RCSB], [http://www.ebi.ac.uk/pdbsum/4ml0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ml0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DINJ_ECOBD DINJ_ECOBD] Antitoxin component of a type II toxin-antitoxin (TA) system (PubMed:24923448). A labile antitoxin that counteracts the effect of cognate toxin YafQ (PubMed:24923448). The YafQ-DinJ heterotetramer binds the consensus sequence 5'-TTTGAGCTACA-3' in the dinJ promoter; DinJ also binds DNA but not as well as the YafQ-DinJ complex (PubMed:24923448). Binding to the dinJ represses expression of the promoter (By similarity).[UniProtKB:Q47150]<ref>PMID:24923448</ref> |
| | <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: Ecobr]] | + | [[Category: Escherichia coli B str. REL606]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dong, Y H]] | + | [[Category: Dong YH]] |
| - | [[Category: Gao, Z Q]] | + | [[Category: Gao ZQ]] |
| - | [[Category: Liang, Y J]] | + | [[Category: Liang YJ]] |
| - | [[Category: Liu, Q S]] | + | [[Category: Liu QS]] |
| - | [[Category: Interferase]]
| + | |
| - | [[Category: Rhh motif]]
| + | |
| - | [[Category: Toxin-antitoxin complex]]
| + | |
| Structural highlights
Function
DINJ_ECOBD Antitoxin component of a type II toxin-antitoxin (TA) system (PubMed:24923448). A labile antitoxin that counteracts the effect of cognate toxin YafQ (PubMed:24923448). The YafQ-DinJ heterotetramer binds the consensus sequence 5'-TTTGAGCTACA-3' in the dinJ promoter; DinJ also binds DNA but not as well as the YafQ-DinJ complex (PubMed:24923448). Binding to the dinJ represses expression of the promoter (By similarity).[UniProtKB:Q47150][1]
Publication Abstract from PubMed
Toxin YafQ functions as a ribonuclease in the dinJ-yafQ toxin-antitoxin system of Escherichia coli. Antitoxin DinJ neutralizes YafQ-mediated toxicity by forming a stable protein complex. Here, crystal structures of the (DinJ)2-(YafQ)2 complex and the isolated YafQ toxin have been determined. The structure of the heterotetrameric complex (DinJ)2-(YafQ)2 revealed that the N-terminal region of DinJ folds into a ribbon-helix-helix motif and dimerizes for DNA recognition, and the C-terminal portion of each DinJ exclusively wraps around a YafQ molecule. Upon incorporation into the heterotetrameric complex, a conformational change of YafQ in close proximity to the catalytic site of the typical microbial ribonuclease fold was observed and validated. Mutagenesis experiments revealed that a DinJ mutant restored YafQ RNase activity in a tetramer complex in vitro, but not in vivo. An electrophoretic mobility shift assay showed that one of the palindromic sequences present in the upstream intergenic region of DinJ served as a binding sequences for both the DinJ-YafQ complex and the antitoxin DinJ alone. Based on structure-guided and site-directed mutagenesis of DinJ-YafQ, we showed that two pairs of amino acids in DinJ were important for DNA binding: The R8A and K16A, and S31A and R35A substitutions in DinJ abolished the DNA binding ability of the DinJ-YafQ complex.
Structural and Functional Characterization of Escherichia coli Toxin-antitoxin Complex DinJ-YafQ.,Liang Y, Gao Z, Wang F, Zhang Y, Dong Y, Liu Q J Biol Chem. 2014 Jun 12. pii: jbc.M114.559773. PMID:24923448[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liang Y, Gao Z, Wang F, Zhang Y, Dong Y, Liu Q. Structural and Functional Characterization of Escherichia coli Toxin-antitoxin Complex DinJ-YafQ. J Biol Chem. 2014 Jun 12. pii: jbc.M114.559773. PMID:24923448 doi:http://dx.doi.org/10.1074/jbc.M114.559773
- ↑ Liang Y, Gao Z, Wang F, Zhang Y, Dong Y, Liu Q. Structural and Functional Characterization of Escherichia coli Toxin-antitoxin Complex DinJ-YafQ. J Biol Chem. 2014 Jun 12. pii: jbc.M114.559773. PMID:24923448 doi:http://dx.doi.org/10.1074/jbc.M114.559773
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