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| | <StructureSection load='6hn7' size='340' side='right'caption='[[6hn7]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='6hn7' size='340' side='right'caption='[[6hn7]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6hn7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895] and [http://en.wikipedia.org/wiki/Bacteriophage_lambda Bacteriophage lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HN7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HN7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6hn7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_virus_Lambda Escherichia virus Lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HN7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HN7 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CXXR01000010.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), Nu1, lambdap01 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10710 Bacteriophage lambda])</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]] 3Å</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=6hn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hn7 OCA], [http://pdbe.org/6hn7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hn7 RCSB], [http://www.ebi.ac.uk/pdbsum/6hn7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hn7 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=6hn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hn7 OCA], [https://pdbe.org/6hn7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hn7 RCSB], [https://www.ebi.ac.uk/pdbsum/6hn7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hn7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TERS_LAMBD TERS_LAMBD]] Component of the terminase that processes and encapsidates viral genomes during virion assembly. The terminase is composed of two small and one large subunits. To initiate packaging, it binds a specific sequence called cos, at the junction of adjacent viral genomes in the concatemeric DNA substrate. Next, in a reaction stimulated by the presence of proheads and ATP but not requiring ATP hydrolysis, the terminase creates two nicks 12bp appart at the cos site, one on each stand. Terminase then separates the cohesive ends in a reaction requiring ATP hydrolysis. The heterotrimer remains bound to the left end of the genome to be packaged, forming a stable DNA-protein complex known as complex I. In a reaction facilitated by a viral assembly catalyst, gpFI, complex I binds a prohead, a preformed head shell precursor, to form complex II. In another packaging reaction requiring ATP hydrolysis, the DNA is translocated into the prohead until the next cos site on the concatemer reaches the packaging complex. At this time the downstream cos site is cut and the heterotrimer undocks from the DNA-filled head to remain bound to the left end of concatemer's next genome. The new heterotrimer-DNA complex I binds another prohead to continue the processive, polarized packaging of viral genomes. The terminase is dependent upon host integration host factor (ihfA/ihfB) for these activities.<ref>PMID:2989542</ref> | + | [https://www.uniprot.org/uniprot/A0A5H1ZR32_ECOLX A0A5H1ZR32_ECOLX] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6hn7" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6hn7" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Terminase 3D Structures|Terminase 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Bacteriophage lambda]] | + | [[Category: Escherichia virus Lambda]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Alqasmi, M]] | + | [[Category: Alqasmi M]] |
| - | [[Category: Bacarizo, J]] | + | [[Category: Bacarizo J]] |
| - | [[Category: Ciges-Tomas, J R]] | + | [[Category: Ciges-Tomas JR]] |
| - | [[Category: Fillol-Salom, A]] | + | [[Category: Fillol-Salom A]] |
| - | [[Category: Marina, A]] | + | [[Category: Marina A]] |
| - | [[Category: Penades, J R]] | + | [[Category: Penades JR]] |
| - | [[Category: Roszak, A W]] | + | [[Category: Roszak AW]] |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Hetero-dimer]]
| + | |
| - | [[Category: Phage interference]]
| + | |
| - | [[Category: Protein complex]]
| + | |
| - | [[Category: Redirecting packaging protein]]
| + | |
| Structural highlights
Function
A0A5H1ZR32_ECOLX
Publication Abstract from PubMed
Phage-inducible chromosomal islands (PICIs) represent a novel and universal class of mobile genetic elements, which have broad impact on bacterial virulence. In spite of their relevance, how the Gram-negative PICIs hijack the phage machinery for their own specific packaging and how they block phage reproduction remains to be determined. Using genetic and structural analyses, we solve the mystery here by showing that the Gram-negative PICIs encode a protein that simultaneously performs these processes. This protein, which we have named Rpp (for redirecting phage packaging), interacts with the phage terminase small subunit, forming a heterocomplex. This complex is unable to recognize the phage DNA, blocking phage packaging, but specifically binds to the PICI genome, promoting PICI packaging. Our studies reveal the mechanism of action that allows PICI dissemination in nature, introducing a new paradigm in the understanding of the biology of pathogenicity islands and therefore of bacterial pathogen evolution.
Hijacking the Hijackers: Escherichia coli Pathogenicity Islands Redirect Helper Phage Packaging for Their Own Benefit.,Fillol-Salom A, Bacarizo J, Alqasmi M, Ciges-Tomas JR, Martinez-Rubio R, Roszak AW, Cogdell RJ, Chen J, Marina A, Penades JR Mol Cell. 2019 Jul 8. pii: S1097-2765(19)30473-3. doi:, 10.1016/j.molcel.2019.06.017. PMID:31350119[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fillol-Salom A, Bacarizo J, Alqasmi M, Ciges-Tomas JR, Martinez-Rubio R, Roszak AW, Cogdell RJ, Chen J, Marina A, Penades JR. Hijacking the Hijackers: Escherichia coli Pathogenicity Islands Redirect Helper Phage Packaging for Their Own Benefit. Mol Cell. 2019 Jul 8. pii: S1097-2765(19)30473-3. doi:, 10.1016/j.molcel.2019.06.017. PMID:31350119 doi:http://dx.doi.org/10.1016/j.molcel.2019.06.017
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