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| <StructureSection load='5i8j' size='340' side='right'caption='[[5i8j]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='5i8j' size='340' side='right'caption='[[5i8j]], [[Resolution|resolution]] 1.75Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5i8j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpr69 Bpr69]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I8J OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5I8J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5i8j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_RB69 Escherichia phage RB69]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I8J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I8J FirstGlance]. <br> |
- | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4i8r|4i8r]]</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]] 1.75Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dmd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=12353 BPR69])</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=5i8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i8j OCA], [https://pdbe.org/5i8j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i8j RCSB], [https://www.ebi.ac.uk/pdbsum/5i8j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i8j ProSAT]</span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5i8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i8j OCA], [http://pdbe.org/5i8j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i8j RCSB], [http://www.ebi.ac.uk/pdbsum/5i8j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i8j ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q7Y599_BPR69 Q7Y599_BPR69] |
| <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: Bpr69]] | + | [[Category: Escherichia phage RB69]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Dong, Y H]] | + | [[Category: Dong YH]] |
- | [[Category: Gao, Z Q]] | + | [[Category: Gao ZQ]] |
- | [[Category: Wei, Y]] | + | [[Category: Wei Y]] |
- | [[Category: Zhang, H]] | + | [[Category: Zhang H]] |
- | [[Category: Antitoxin]]
| + | |
| Structural highlights
Function
Q7Y599_BPR69
Publication Abstract from PubMed
Toxin-antitoxin (TA) loci are widespread in bacteria plasmids and chromosomes, and target various cellular functions to regulate cell growth and death. A type II TA system RnlA-RnlB from Escherichia coli is associated with phage-resistance. After the infection of bacteriophage T4 with Dmd defection, RnlA is activated by the disappearance of RnlB, resulting in the rapid degradation of T4 mRNAs. Dmd can bind to RnlA directly and neutralize RnlA toxicity to allow phage reproduction. Dmd represent a heterogenous antitoxin of RnlA replacing antitoxin RnlB. Here, we reported two structures of Dmd from T4 phage and RB69 phage. Both Dmd structures are high similar with a compacted domain composed of a four-stranded anti-parallel beta-sheet and an alpha-helix. Chromatography and SAXS suggest Dmd forms a dimer in solution consistent with that in crystal. Structure-based mutagenesis of Dmd reveals key residues involved in RnlA-binding. Possibility cavities in Dmd used for compounds design were modeled. Our structural study revealed the recognition and inhibition mechanism of RnlA by Dmd and providing a potential laboratory phage prevention target for drug design.
Structural characterizations of phage antitoxin Dmd and its interactions with bacterial toxin RnlA.,Wei Y, Gao Z, Zhang H, Dong Y Biochem Biophys Res Commun. 2016 Apr 15;472(4):592-7. doi:, 10.1016/j.bbrc.2016.03.025. Epub 2016 Mar 10. PMID:26972252[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wei Y, Gao Z, Zhang H, Dong Y. Structural characterizations of phage antitoxin Dmd and its interactions with bacterial toxin RnlA. Biochem Biophys Res Commun. 2016 Apr 15;472(4):592-7. doi:, 10.1016/j.bbrc.2016.03.025. Epub 2016 Mar 10. PMID:26972252 doi:http://dx.doi.org/10.1016/j.bbrc.2016.03.025
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