6nm5
From Proteopedia
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== 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> | [[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> | ||
| + | <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. | ||
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| + | 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> | ||
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| + | 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/> | ||
Revision as of 07:00, 31 July 2019
F-pilus/MS2 Maturation protein complex
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