Crystal Structure of the Maturation Protein from Bacteriophage Qβ

Virions of the single-stranded RNA bacteriophages contain a single copy of the maturation protein, which is bound to the phage genome and is required for the infectivity of the particles. The maturation protein mediates the adsorption of the virion to bacterial pili and the subsequent release and pe...

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Vydáno v:	Journal of molecular biology Ročník 429; číslo 5; s. 688 - 696
Hlavní autoři:	Rumnieks, Janis, Tars, Kaspars
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	England Elsevier Ltd 10.03.2017
Témata:	adsorption Amino Acid Sequence bacteria bacteriophages Bacteriophages - chemistry Bacteriophages - genetics capsid Capsid Proteins - chemistry Capsid Proteins - genetics Cloning, Molecular coat proteins Cryoelectron Microscopy crystal structure evolution fimbriae Gene Expression Regulation, Viral genome Leviviridae maturation protein pathogenicity Protein Conformation protein structure RNA RNA phages RNA Phages - chemistry RNA Phages - genetics RNA, Viral - chemistry RNA, Viral - genetics virion Virion - chemistry Virion - genetics virus structure maturation protein MBP SeMet virus structure cryo-EM RNA phages Qß ssRNA
ISSN:	0022-2836, 1089-8638, 1089-8638
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Abstract	Virions of the single-stranded RNA bacteriophages contain a single copy of the maturation protein, which is bound to the phage genome and is required for the infectivity of the particles. The maturation protein mediates the adsorption of the virion to bacterial pili and the subsequent release and penetration of the genome into the host cell. Here, we report a crystal structure of the maturation protein from bacteriophage Qβ. The protein has a bent, highly asymmetric shape and spans 110Å in length. Apart from small local substructures, the overall fold of the maturation protein does not resemble that of other known proteins. The protein is organized in two distinct regions, an α-helical part with a four-helix core, and a β stranded part that contains a seven-stranded sheet in the central part and a five-stranded sheet at the tip of the protein. The Qβ maturation protein has two distinct, positively charged areas at opposite sides of the α-helical part, which are involved in genomic RNA binding. The maturation protein binds to each of the surrounding coat protein dimers in the capsid differently, and the interaction is considerably weaker compared to coat protein interdimer contacts. The coat protein- or RNA-binding residues are not preserved among different ssRNA phage maturation proteins; instead, the distal end of the α-helical part is the most evolutionarily conserved, suggesting the importance of this region for maintaining the functionality of the protein. [Display omitted] •Crystal structure of the maturation protein from bacteriophage Qβ solved at 3.3-Å resolution•The maturation protein consists of a conserved helical and a variable beta sheet region.•The obtained structure fitted into a recently published low-resolution asymmetric cryo-electron microscopy (EM) map of bacteriophage Qβ.•Regions of the maturation protein, involved in coat protein and RNA binding, are identified.
AbstractList	Virions of the single-stranded RNA bacteriophages contain a single copy of the maturation protein, which is bound to the phage genome and is required for the infectivity of the particles. The maturation protein mediates the adsorption of the virion to bacterial pili and the subsequent release and penetration of the genome into the host cell. Here, we report a crystal structure of the maturation protein from bacteriophage Qβ. The protein has a bent, highly asymmetric shape and spans 110Å in length. Apart from small local substructures, the overall fold of the maturation protein does not resemble that of other known proteins. The protein is organized in two distinct regions, an α-helical part with a four-helix core, and a β stranded part that contains a seven-stranded sheet in the central part and a five-stranded sheet at the tip of the protein. The Qβ maturation protein has two distinct, positively charged areas at opposite sides of the α-helical part, which are involved in genomic RNA binding. The maturation protein binds to each of the surrounding coat protein dimers in the capsid differently, and the interaction is considerably weaker compared to coat protein interdimer contacts. The coat protein- or RNA-binding residues are not preserved among different ssRNA phage maturation proteins; instead, the distal end of the α-helical part is the most evolutionarily conserved, suggesting the importance of this region for maintaining the functionality of the protein. [Display omitted] •Crystal structure of the maturation protein from bacteriophage Qβ solved at 3.3-Å resolution•The maturation protein consists of a conserved helical and a variable beta sheet region.•The obtained structure fitted into a recently published low-resolution asymmetric cryo-electron microscopy (EM) map of bacteriophage Qβ.•Regions of the maturation protein, involved in coat protein and RNA binding, are identified. Virions of the single-stranded RNA bacteriophages contain a single copy of the maturation protein, which is bound to the phage genome and is required for the infectivity of the particles. The maturation protein mediates the adsorption of the virion to bacterial pili and the subsequent release and penetration of the genome into the host cell. Here, we report a crystal structure of the maturation protein from bacteriophage Qβ. The protein has a bent, highly asymmetric shape and spans 110Å in length. Apart from the small local substructures, the overall fold of the maturation protein does not resemble that of other known proteins. The protein is organized in two distinct regions, an α-helical part with a four-helix core, and a β stranded part that contains a seven-stranded sheet in the central part and a five-stranded sheet at the tip of the protein. The Qβ maturation protein has two distinct, positively charged areas at opposite sides of the α-helical part, which are involved in genomic RNA binding. The maturation protein binds to each of the surrounding coat protein dimers in the capsid differently, and the interaction is considerably weaker compared to coat protein interdimer contacts. The coat protein- or RNA-binding residues are not preserved among different ssRNA phage maturation proteins; instead, the distal end of the α-helical part is the most evolutionarily conserved, suggesting the importance of this region for maintaining the functionality of the protein. Virions of the single-stranded RNA bacteriophages contain a single copy of the maturation protein, which is bound to the phage genome and is required for the infectivity of the particles. The maturation protein mediates the adsorption of the virion to bacterial pili and the subsequent release and penetration of the genome into the host cell. Here, we report a crystal structure of the maturation protein from bacteriophage Qβ. The protein has a bent, highly asymmetric shape and spans 110Å in length. Apart from small local substructures, the overall fold of the maturation protein does not resemble that of other known proteins. The protein is organized in two distinct regions, an α-helical part with a four-helix core, and a β stranded part that contains a seven-stranded sheet in the central part and a five-stranded sheet at the tip of the protein. The Qβ maturation protein has two distinct, positively charged areas at opposite sides of the α-helical part, which are involved in genomic RNA binding. The maturation protein binds to each of the surrounding coat protein dimers in the capsid differently, and the interaction is considerably weaker compared to coat protein interdimer contacts. The coat protein- or RNA-binding residues are not preserved among different ssRNA phage maturation proteins; instead, the distal end of the α-helical part is the most evolutionarily conserved, suggesting the importance of this region for maintaining the functionality of the protein. Virions of the single-stranded RNA bacteriophages contain a single copy of the maturation protein, which is bound to the phage genome and is required for the infectivity of the particles. The maturation protein mediates the adsorption of the virion to bacterial pili and the subsequent release and penetration of the genome into the host cell. Here, we report a crystal structure of the maturation protein from bacteriophage Qβ. The protein has a bent, highly asymmetric shape and spans 110Å in length. Apart from small local substructures, the overall fold of the maturation protein does not resemble that of other known proteins. The protein is organized in two distinct regions, an α-helical part with a four-helix core, and a β stranded part that contains a seven-stranded sheet in the central part and a five-stranded sheet at the tip of the protein. The Qβ maturation protein has two distinct, positively charged areas at opposite sides of the α-helical part, which are involved in genomic RNA binding. The maturation protein binds to each of the surrounding coat protein dimers in the capsid differently, and the interaction is considerably weaker compared to coat protein interdimer contacts. The coat protein- or RNA-binding residues are not preserved among different ssRNA phage maturation proteins; instead, the distal end of the α-helical part is the most evolutionarily conserved, suggesting the importance of this region for maintaining the functionality of the protein.Virions of the single-stranded RNA bacteriophages contain a single copy of the maturation protein, which is bound to the phage genome and is required for the infectivity of the particles. The maturation protein mediates the adsorption of the virion to bacterial pili and the subsequent release and penetration of the genome into the host cell. Here, we report a crystal structure of the maturation protein from bacteriophage Qβ. The protein has a bent, highly asymmetric shape and spans 110Å in length. Apart from small local substructures, the overall fold of the maturation protein does not resemble that of other known proteins. The protein is organized in two distinct regions, an α-helical part with a four-helix core, and a β stranded part that contains a seven-stranded sheet in the central part and a five-stranded sheet at the tip of the protein. The Qβ maturation protein has two distinct, positively charged areas at opposite sides of the α-helical part, which are involved in genomic RNA binding. The maturation protein binds to each of the surrounding coat protein dimers in the capsid differently, and the interaction is considerably weaker compared to coat protein interdimer contacts. The coat protein- or RNA-binding residues are not preserved among different ssRNA phage maturation proteins; instead, the distal end of the α-helical part is the most evolutionarily conserved, suggesting the importance of this region for maintaining the functionality of the protein.
Author	Tars, Kaspars Rumnieks, Janis
Author_xml	– sequence: 1 givenname: Janis surname: Rumnieks fullname: Rumnieks, Janis organization: Biomedical Research and Study Center, Ratsupites 1, LV1067 Riga, Latvia – sequence: 2 givenname: Kaspars surname: Tars fullname: Tars, Kaspars email: kaspars@biomed.lu.lv organization: Biomedical Research and Study Center, Ratsupites 1, LV1067 Riga, Latvia
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Cites_doi	10.1093/nar/gkq366 10.1016/0042-6822(71)90176-0 10.1016/j.jmb.2007.05.022 10.1016/0022-2836(68)90329-X 10.1016/0092-8674(79)90045-X 10.1107/S0907444996012255 10.1107/S0108767307043930 10.1016/0042-6822(72)90552-1 10.1093/nar/gkv332 10.1002/j.1460-2075.1983.tb01617.x 10.1107/S0907444910045749 10.1006/jmbi.1993.1407 10.1016/j.str.2013.05.012 10.1016/0005-2787(81)90179-9 10.1107/S0907444904019158 10.1107/S0907444909042073 10.1016/0042-6822(64)90063-7 10.1016/0092-8674(79)90044-8 10.1073/pnas.1609482113 10.1038/newbio234206a0 10.1093/nar/gkh340 10.1126/science.1058289 10.1016/0005-2787(74)90366-9 10.1016/0092-8674(83)90030-2 10.1111/mmi.12021 10.1107/S0907444909047337 10.1038/ncomms12524 10.1107/S0021889812011715
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Snippet	Virions of the single-stranded RNA bacteriophages contain a single copy of the maturation protein, which is bound to the phage genome and is required for the...
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SubjectTerms	adsorption Amino Acid Sequence bacteria bacteriophages Bacteriophages - chemistry Bacteriophages - genetics capsid Capsid Proteins - chemistry Capsid Proteins - genetics Cloning, Molecular coat proteins Cryoelectron Microscopy crystal structure evolution fimbriae Gene Expression Regulation, Viral genome Leviviridae maturation protein pathogenicity Protein Conformation protein structure RNA RNA phages RNA Phages - chemistry RNA Phages - genetics RNA, Viral - chemistry RNA, Viral - genetics virion Virion - chemistry Virion - genetics virus structure
Title	Crystal Structure of the Maturation Protein from Bacteriophage Qβ
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