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| | <SX load='6nm5' size='340' side='right' viewer='molstar' caption='[[6nm5]], [[Resolution|resolution]] 6.20Å' scene=''> | | <SX load='6nm5' size='340' side='right' viewer='molstar' caption='[[6nm5]], [[Resolution|resolution]] 6.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6nm5]] is a 76 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_ms2 Enterobacteria phage ms2] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NM5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6NM5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6nm5]] is a 76 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_virus_MS2 Escherichia virus MS2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NM5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NM5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KSV:(2R)-2,3-dihydroxypropyl+ethyl+hydrogen+(S)-phosphate'>KSV</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.2Å</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=6nm5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nm5 OCA], [http://pdbe.org/6nm5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nm5 RCSB], [http://www.ebi.ac.uk/pdbsum/6nm5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nm5 ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KSV:(2R)-2,3-dihydroxypropyl+ethyl+hydrogen+(S)-phosphate'>KSV</scene></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=6nm5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nm5 OCA], [https://pdbe.org/6nm5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nm5 RCSB], [https://www.ebi.ac.uk/pdbsum/6nm5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nm5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MAT_BPMS2 MAT_BPMS2]] The maturation protein is required for the typical attachment of the phage to the side of the bacterial pili (PubMed:23810697). MP binds to sequences located toward each end of the genome, hence circularizing it (PubMed:26608810). The RNA genome-MP complex is released from the capsid upon host receptor binding (PubMed:23810697). MP enters the cell along with the viral RNA (PubMed:4551992).<ref>PMID:23810697</ref> <ref>PMID:26608810</ref> <ref>PMID:4551992</ref> | + | [https://www.uniprot.org/uniprot/MATA_BPMS2 MATA_BPMS2] The maturation protein is required for the typical attachment of the phage to the side of the bacterial pili (PubMed:23810697). Binds to sequences located toward each end of the genome, hence circularizing it (PubMed:26608810). The RNA genome-maturation protein A complex is released from the capsid upon host receptor binding (PubMed:23810697). Maturation protein A enters the cell along with the viral RNA (PubMed:4551992).<ref>PMID:23810697</ref> <ref>PMID:26608810</ref> <ref>PMID:4551992</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Single-stranded RNA bacteriophages (ssRNA phages) infect Gram-negative bacteria via a single maturation protein (Mat), which attaches to a retractile pilus of the host. Here we present structures of the ssRNA phage MS2 in complex with the Escherichia coli F-pilus, showing a network of hydrophobic and electrostatic interactions at the Mat-pilus interface. Moreover, binding of the pilus induces slight orientational variations of the Mat relative to the rest of the phage capsid, priming the Mat-connected genomic RNA (gRNA) for its release from the virions. The exposed tip of the attached Mat points opposite to the direction of the pilus retraction, which may facilitate the translocation of the gRNA from the capsid into the host cytosol. In addition, our structures determine the orientation of the assembled F-pilin subunits relative to the cell envelope, providing insights into the F-like type IV secretion systems.
| + | |
| - | | + | |
| - | Structural basis for the adsorption of a single-stranded RNA bacteriophage.,Meng R, Jiang M, Cui Z, Chang JY, Yang K, Jakana J, Yu X, Wang Z, Hu B, Zhang J Nat Commun. 2019 Jul 16;10(1):3130. doi: 10.1038/s41467-019-11126-8. PMID:31311931<ref>PMID:31311931</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6nm5" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Enterobacteria phage ms2]] | |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| | + | [[Category: Escherichia virus MS2]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chang, J]] | + | [[Category: Chang J]] |
| - | [[Category: Meng, R]] | + | [[Category: Meng R]] |
| - | [[Category: Zhang, J]] | + | [[Category: Zhang J]] |
| - | [[Category: Adsorption complex]]
| + | |
| - | [[Category: F-pilus]]
| + | |
| - | [[Category: Ms2 maturation protein]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
MATA_BPMS2 The maturation protein is required for the typical attachment of the phage to the side of the bacterial pili (PubMed:23810697). Binds to sequences located toward each end of the genome, hence circularizing it (PubMed:26608810). The RNA genome-maturation protein A complex is released from the capsid upon host receptor binding (PubMed:23810697). Maturation protein A enters the cell along with the viral RNA (PubMed:4551992).[1] [2] [3]
References
- ↑ Dent KC, Thompson R, Barker AM, Hiscox JA, Barr JN, Stockley PG, Ranson NA. The Asymmetric Structure of an Icosahedral Virus Bound to Its Receptor Suggests a Mechanism for Genome Release. Structure. 2013 Jun 25. pii: S0969-2126(13)00194-9. doi:, 10.1016/j.str.2013.05.012. PMID:23810697 doi:10.1016/j.str.2013.05.012
- ↑ Rolfsson O, Middleton S, Manfield IW, White SJ, Fan B, Vaughan R, Ranson NA, Dykeman E, Twarock R, Ford J, Kao CC, Stockley PG. Direct Evidence for Packaging Signal-Mediated Assembly of Bacteriophage MS2. J Mol Biol. 2016 Jan 29;428(2 Pt B):431-48. doi: 10.1016/j.jmb.2015.11.014. Epub , 2015 Dec 1. PMID:26608810 doi:http://dx.doi.org/10.1016/j.jmb.2015.11.014
- ↑ Krahn PM, O'Callaghan RJ, Paranchych W. Stages in phage R17 infection. VI. Injection of A protein and RNA into the host cell. Virology. 1972 Mar;47(3):628-37. PMID:4551992
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