Conformational Polymorphism of m7GTP in Crystal Structure of the PB2 Middle Domain from Human Influenza A Virus
Identifieur interne : 000902 ( Main/Exploration ); précédent : 000901; suivant : 000903Conformational Polymorphism of m7GTP in Crystal Structure of the PB2 Middle Domain from Human Influenza A Virus
Auteurs : Toshiharu Tsurumura [Japon] ; Hao Qiu [Japon] ; Toru Yoshida [Japon] ; Yayoi Tsumori [Japon] ; Dai Hatakeyama [Japon] ; Takashi Kuzuhara [Japon] ; Hideaki Tsuge [Japon]Source :
- PLoS ONE [ 1932-6203 ] ; 2013.
Abstract
Influenza pandemics with human-to-human transmission of the virus are of great public concern. It is now recognized that a number of factors are necessary for human transmission and virulence, including several key mutations within the PB2 subunit of RNA-dependent RNA polymerase. The structure of the middle domain in PB2 has been revealed with or without m7GTP, thus the middle domain is considered to be novel target for structure-based drug design. Here we report the crystal structure of the middle domain of H1N1 PB2 with or without m7GTP at 1.9Å and 2.0Å resolution, respectively, which has two mutations (P453H, I471T) to increase electrostatic potential and solubility. Here we report the m7GTP has unique conformation differ from the reported structure. 7-methyl-guanine is fixed in the pocket, but particularly significant change is seen in ribose and triphosphate region: the buried 7-methyl-guanine indeed binds in the pocket forming by H357, F404, E361 and K376 but the triphosphate continues directly to the outer domain. The presented conformation of m7GTP may be a clue for the anti-influenza drug-design.
Url:
DOI: 10.1371/journal.pone.0082020
PubMed: 24312396
PubMed Central: 3843726
Affiliations:
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the PB2 Middle Domain from Human Influenza A Virus</title><author><name sortKey="Tsurumura, Toshiharu" sort="Tsurumura, Toshiharu" uniqKey="Tsurumura T" first="Toshiharu" last="Tsurumura">Toshiharu Tsurumura</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto, Japan</addr-line></nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto</wicri:regionArea><wicri:noRegion>Kyoto</wicri:noRegion></affiliation></author><author><name sortKey="Qiu, Hao" sort="Qiu, Hao" uniqKey="Qiu H" first="Hao" last="Qiu">Hao Qiu</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto, Japan</addr-line></nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto</wicri:regionArea><wicri:noRegion>Kyoto</wicri:noRegion></affiliation></author><author><name sortKey="Yoshida, Toru" sort="Yoshida, Toru" uniqKey="Yoshida T" first="Toru" last="Yoshida">Toru Yoshida</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto, Japan</addr-line></nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto</wicri:regionArea><wicri:noRegion>Kyoto</wicri:noRegion></affiliation></author><author><name sortKey="Tsumori, Yayoi" sort="Tsumori, Yayoi" uniqKey="Tsumori Y" first="Yayoi" last="Tsumori">Yayoi Tsumori</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto, Japan</addr-line></nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto</wicri:regionArea><wicri:noRegion>Kyoto</wicri:noRegion></affiliation></author><author><name sortKey="Hatakeyama, Dai" sort="Hatakeyama, Dai" uniqKey="Hatakeyama D" first="Dai" last="Hatakeyama">Dai Hatakeyama</name><affiliation wicri:level="1"><nlm:aff id="aff2"><addr-line>Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Tokushima, Japan</addr-line></nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Tokushima</wicri:regionArea><wicri:noRegion>Tokushima</wicri:noRegion></affiliation></author><author><name sortKey="Kuzuhara, Takashi" sort="Kuzuhara, Takashi" uniqKey="Kuzuhara T" first="Takashi" last="Kuzuhara">Takashi Kuzuhara</name><affiliation wicri:level="1"><nlm:aff id="aff2"><addr-line>Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Tokushima, Japan</addr-line></nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Tokushima</wicri:regionArea><wicri:noRegion>Tokushima</wicri:noRegion></affiliation></author><author><name sortKey="Tsuge, Hideaki" sort="Tsuge, Hideaki" uniqKey="Tsuge H" first="Hideaki" last="Tsuge">Hideaki Tsuge</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto, Japan</addr-line></nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto</wicri:regionArea><wicri:noRegion>Kyoto</wicri:noRegion></affiliation></author></analytic><series><title level="j">PLoS ONE</title><idno type="eISSN">1932-6203</idno><imprint><date when="2013">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Influenza pandemics with human-to-human transmission of the virus are of great public concern. It is now recognized that a number of factors are necessary for human transmission and virulence, including several key mutations within the PB2 subunit of RNA-dependent RNA polymerase. The structure of the middle domain in PB2 has been revealed with or without m<sup>7</sup>GTP, thus the middle domain is considered to be novel target for structure-based drug design. Here we report the crystal structure of the middle domain of H1N1 PB2 with or without m<sup>7</sup>GTP at 1.9Å and 2.0Å resolution, respectively, which has two mutations (P453H, I471T) to increase electrostatic potential and solubility. Here we report the m<sup>7</sup>GTP has unique conformation differ from the reported structure. 7-methyl-guanine is fixed in the pocket, but particularly significant change is seen in ribose and triphosphate region: the buried 7-methyl-guanine indeed binds in the pocket forming by H357, F404, E361 and K376 but the triphosphate continues directly to the outer domain. The presented conformation of m<sup>7</sup>GTP may be a clue for the anti-influenza drug-design.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Reid, Ah" uniqKey="Reid A">AH Reid</name></author><author><name sortKey="Taubenberger, Jk" uniqKey="Taubenberger J">JK Taubenberger</name></author><author><name sortKey="Fanning, Tg" uniqKey="Fanning T">TG Fanning</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Elton, D" uniqKey="Elton D">D Elton</name></author><author><name sortKey="Digard, P" uniqKey="Digard P">P Digard</name></author><author><name sortKey="Tiley, L" uniqKey="Tiley L">L Tiley</name></author><author><name sortKey="Ortin, J" uniqKey="Ortin J">J Ortin</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Plotch, Sj" uniqKey="Plotch S">SJ Plotch</name></author><author><name sortKey="Bouloy, M" uniqKey="Bouloy M">M Bouloy</name></author><author><name 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Pd" uniqKey="Adams P">PD Adams</name></author><author><name sortKey="Afonine, Pv" uniqKey="Afonine P">PV Afonine</name></author><author><name sortKey="Bunk Czi, G" uniqKey="Bunk Czi G">G Bunkóczi</name></author><author><name sortKey="Chen, Vb" uniqKey="Chen V">VB Chen</name></author><author><name sortKey="Davis, Iw" uniqKey="Davis I">IW Davis</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>Japon</li></country></list><tree><country name="Japon"><noRegion><name sortKey="Tsurumura, Toshiharu" sort="Tsurumura, Toshiharu" uniqKey="Tsurumura T" first="Toshiharu" last="Tsurumura">Toshiharu Tsurumura</name></noRegion><name sortKey="Hatakeyama, Dai" sort="Hatakeyama, Dai" uniqKey="Hatakeyama D" first="Dai" last="Hatakeyama">Dai Hatakeyama</name><name sortKey="Kuzuhara, Takashi" sort="Kuzuhara, Takashi" uniqKey="Kuzuhara T" first="Takashi" last="Kuzuhara">Takashi Kuzuhara</name><name sortKey="Qiu, Hao" sort="Qiu, Hao" uniqKey="Qiu H" first="Hao" last="Qiu">Hao Qiu</name><name sortKey="Tsuge, Hideaki" sort="Tsuge, Hideaki" uniqKey="Tsuge H" first="Hideaki" last="Tsuge">Hideaki Tsuge</name><name sortKey="Tsumori, Yayoi" sort="Tsumori, Yayoi" uniqKey="Tsumori Y" first="Yayoi" last="Tsumori">Yayoi Tsumori</name><name sortKey="Yoshida, Toru" sort="Yoshida, Toru" uniqKey="Yoshida T" first="Toru" last="Yoshida">Toru Yoshida</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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