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| ==The response regulator TorI belongs to a new family of atypical excisionase== | | ==The response regulator TorI belongs to a new family of atypical excisionase== |
- | <StructureSection load='1z4h' size='340' side='right'caption='[[1z4h]], [[NMR_Ensembles_of_Models | 17 NMR models]]' scene=''> | + | <StructureSection load='1z4h' size='340' side='right'caption='[[1z4h]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1z4h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z4H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z4H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1z4h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z4H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z4H FirstGlance]. <br> |
- | </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=1z4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z4h OCA], [http://pdbe.org/1z4h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z4h RCSB], [http://www.ebi.ac.uk/pdbsum/1z4h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z4h ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1z4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z4h OCA], [https://pdbe.org/1z4h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z4h RCSB], [https://www.ebi.ac.uk/pdbsum/1z4h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z4h ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/VXIS_BPHK6 VXIS_BPHK6]] Excisionase and integrase are necessary for the excision of prophage from the host genome by site-specific recombination at the att site (By similarity). | + | [https://www.uniprot.org/uniprot/TORI_ECOLI TORI_ECOLI] Transcription inhibitory protein for the torCAD operon. Also acts as an excisionase and plays an essential role in the defective prophage CPS53 excision.<ref>PMID:15197250</ref> <ref>PMID:16079126</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: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Ansaldi, M]] | + | [[Category: Ansaldi M]] |
- | [[Category: Elantak, L]] | + | [[Category: Elantak L]] |
- | [[Category: Guerlesquin, F]] | + | [[Category: Guerlesquin F]] |
- | [[Category: Mejean, V]] | + | [[Category: Mejean V]] |
- | [[Category: Morelli, X]] | + | [[Category: Morelli X]] |
- | [[Category: Dna binding protein]]
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- | [[Category: Protein binding]]
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- | [[Category: Reverse turn]]
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- | [[Category: Winged helix]]
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| Structural highlights
Function
TORI_ECOLI Transcription inhibitory protein for the torCAD operon. Also acts as an excisionase and plays an essential role in the defective prophage CPS53 excision.[1] [2]
Publication Abstract from PubMed
TorI (Tor inhibition protein) has been identified in Escherichia coli as a protein inhibitor acting through protein-protein interaction with the TorR response regulator. This interaction, which does not interfere with TorR DNA binding activity, probably prevents the recruitment of RNA polymerase to the torC promoter. In this study we have solved the solution structure of TorI, which adopts a prokaryotic winged-helix arrangement. Despite no primary sequence similarity, the three-dimensional structure of TorI is highly homologous to the (lambda)Xis, Mu bacteriophage repressor (MuR-DBD), and transposase (MuA-DBD) structures. We propose that the TorI protein is the structural missing link between the (lambda)Xis and MuR proteins. Moreover, in vivo assays demonstrated that TorI plays an essential role in prophage excision. Heteronuclear NMR experiments and site-directed mutagenesis studies have pinpointed out key residues involved in the DNA binding activity of TorI. Our findings suggest that TorI-related proteins identified in various pathogenic bacterial genomes define a new family of atypical excisionases.
Structural and genetic analyses reveal a key role in prophage excision for the TorI response regulator inhibitor.,Elantak L, Ansaldi M, Guerlesquin F, Mejean V, Morelli X J Biol Chem. 2005 Nov 4;280(44):36802-8. Epub 2005 Aug 2. PMID:16079126[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ansaldi M, Théraulaz L, Méjean V. TorI, a response regulator inhibitor of phage origin in Escherichia coli. Proc Natl Acad Sci U S A. 2004 Jun 22;101(25):9423-8. PMID:15197250 doi:10.1073/pnas.0401927101
- ↑ Elantak L, Ansaldi M, Guerlesquin F, Mejean V, Morelli X. Structural and genetic analyses reveal a key role in prophage excision for the TorI response regulator inhibitor. J Biol Chem. 2005 Nov 4;280(44):36802-8. Epub 2005 Aug 2. PMID:16079126 doi:http://dx.doi.org/M507409200
- ↑ Elantak L, Ansaldi M, Guerlesquin F, Mejean V, Morelli X. Structural and genetic analyses reveal a key role in prophage excision for the TorI response regulator inhibitor. J Biol Chem. 2005 Nov 4;280(44):36802-8. Epub 2005 Aug 2. PMID:16079126 doi:http://dx.doi.org/M507409200
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