|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5ifg' size='340' side='right'caption='[[5ifg]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='5ifg' size='340' side='right'caption='[[5ifg]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ifg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IFG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5IFG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ifg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IFG FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.702Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">higB, ygjN, b3083, JW3054 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), higA, ygjM, b3082, JW3053 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5ifg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ifg OCA], [http://pdbe.org/5ifg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ifg RCSB], [http://www.ebi.ac.uk/pdbsum/5ifg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ifg ProSAT]</span></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=5ifg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ifg OCA], [https://pdbe.org/5ifg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ifg RCSB], [https://www.ebi.ac.uk/pdbsum/5ifg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ifg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HIGB_ECOLI HIGB_ECOLI]] Toxic component of a toxin-antitoxin (TA) module. A probable translation-dependent mRNA interferase. Overexpression causes cessation of cell growth and inhibits cell proliferation via inhibition of translation; this blockage is overcome by subsequent expression of antitoxin HigA. Overexpression causes cleavage of a number of mRNAs in a translation-dependent fashion, suggesting this is an mRNA interferase.<ref>PMID:19943910</ref> [[http://www.uniprot.org/uniprot/HIGA_ECOLI HIGA_ECOLI]] Antitoxin component of a toxin-antitoxin (TA) module. Functions as an mRNA interferase antitoxin; overexpression prevents HigB-mediated cessation of cell growth and inhibition of cell proliferation.<ref>PMID:19943910</ref> | + | [https://www.uniprot.org/uniprot/HIGB_ECOLI HIGB_ECOLI] Toxic component of a toxin-antitoxin (TA) module. A probable translation-dependent mRNA interferase. Overexpression causes cessation of cell growth and inhibits cell proliferation via inhibition of translation; this blockage is overcome by subsequent expression of antitoxin HigA. Overexpression causes cleavage of a number of mRNAs in a translation-dependent fashion, suggesting this is an mRNA interferase.<ref>PMID:19943910</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dong, Y H]] | + | [[Category: Dong YH]] |
| - | [[Category: Gao, z Q]] | + | [[Category: Gao zQ]] |
| - | [[Category: Liu, Q S]] | + | [[Category: Liu QS]] |
| - | [[Category: Yang, J S]] | + | [[Category: Yang JS]] |
| - | [[Category: Zhou, K]] | + | [[Category: Zhou K]] |
| - | [[Category: Hydrolase-antitoxin complex]]
| + | |
| - | [[Category: Mrna interferase]]
| + | |
| Structural highlights
Function
HIGB_ECOLI Toxic component of a toxin-antitoxin (TA) module. A probable translation-dependent mRNA interferase. Overexpression causes cessation of cell growth and inhibits cell proliferation via inhibition of translation; this blockage is overcome by subsequent expression of antitoxin HigA. Overexpression causes cleavage of a number of mRNAs in a translation-dependent fashion, suggesting this is an mRNA interferase.[1]
Publication Abstract from PubMed
The toxin-antitoxin system is ubiquitously existed in bacteria and archaea, performing a wide variety of functions modulating cell fitness in response to environmental cues. In this report, we solved the crystal structure of the toxin-antitoxin HigBA complex from E. coli K-12 to 2.7 A resolution. The crystal structure of the HigBA complex displays a hetero-tetramer (HigBA)2 form comprised by two HigB and two HigA subunits. Each toxin HigB resumes a microbial RNase T1 fold, characteristic of a three antiparallel beta-sheet core shielded by a few alpha-helices at either side. Each antitoxin HigA composed of all alpha-helices resembles a "C"-shaped clamp nicely encompassing a HigB in the (HigBA)2 complex. Two HigA monomers dimerize at their N-terminal domain. We showed that HigA helix alpha1 was essential for HigA dimerization and the hetero-tetramer (HigBA)2 formation, but not for a hetero-dimeric HigBA formation. HigA dimerization mediated by helix alpha1 was dispensable for DNA-binding, as a heterodimeric HigBA complex still bound to the higBA operator in vitro. The HigA C-terminal domain with a helix-turn-helix fold was essential for DNA binding. We also defined two palindromes in higBA operator specifically recognized by HigA and HigBA in vitro.
Structural insight into the E. coli HigBA complex.,Yang J, Zhou K, Liu P, Dong Y, Gao Z, Zhang J, Liu Q Biochem Biophys Res Commun. 2016 Sep 30;478(4):1521-7. doi:, 10.1016/j.bbrc.2016.08.131. Epub 2016 Sep 4. PMID:27601326[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Christensen-Dalsgaard M, Jorgensen MG, Gerdes K. Three new RelE-homologous mRNA interferases of Escherichia coli differentially induced by environmental stresses. Mol Microbiol. 2010 Jan;75(2):333-48. doi: 10.1111/j.1365-2958.2009.06969.x. Epub, 2009 Nov 25. PMID:19943910 doi:http://dx.doi.org/10.1111/j.1365-2958.2009.06969.x
- ↑ Yang J, Zhou K, Liu P, Dong Y, Gao Z, Zhang J, Liu Q. Structural insight into the E. coli HigBA complex. Biochem Biophys Res Commun. 2016 Sep 30;478(4):1521-7. doi:, 10.1016/j.bbrc.2016.08.131. Epub 2016 Sep 4. PMID:27601326 doi:http://dx.doi.org/10.1016/j.bbrc.2016.08.131
|
