HK97 PHAGE PORTAL

这个子项目是利用资源的许多研究子项目之一。 由NIH/NCRR资助的中心拨款提供。对子项目的主要支持 子项目的首席调查员可能是由其他来源提供的， 包括美国国立卫生研究院的其他来源。为子项目列出的总成本可能 表示该子项目使用的中心基础设施的估计数量， 不是由NCRR赠款提供给次级项目或次级项目工作人员的直接资金。 在大的dsDNA病毒组装过程中，病毒DNA被转移到预先形成的蛋白质壳中。 DNA包装是由三磷酸腺苷驱动的易位马达系统驱动进入外壳的 水解液。包装机的一个关键部件是门户蛋白。到目前为止，有有限的 门户的详细结构信息，因为只有两个门户噬菌体SPP1和Phi*29噬菌体 门户已经确定。我们已经确定了双环的第一个晶体结构。 链DNA噬菌体HK97样连接器，分辨率为2.9A。 这种400 kDa的马达蛋白将噬菌体的头部和尾巴连接起来，并将 在包装过程中将DNA插入前部。每个单体都有一个细长的形状，并且 由中心的α-螺旋结构域组成，该结构域包括远端的α/β结构域和 近端六链SH3样结构域。原生生物组装成一个12聚体的漏斗状 具有40A宽中央通道的结构。航道的表面主要是 电负性，但它包括三个带正电的环，一个在 漏斗，第二个在粒子的中间，第三个在入口的出口处。 我们希望将晶体结构与大分子成像相结合，以便 广泛地描述这种门户结构。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. During large dsDNA virus assembly, viral DNA is transferred into preformed protein shells. The DNA packaging is driven into the shell by a translocation motor system powered by ATP hydrolysis. A crucial part of the packaging machine is a portal protein. To date there is limited detail structural information of portals as only two portal phages SPP1 and phi*29 phage portals have been determined. We have determined the first crystal structure of the double- stranded DNA bacteriophage HK97-like connector to 2.9 A resolution. This 400 kDa motor protein connects the head of the phage to its tail and translocates the DNA into the prohead during packaging. Each monomer has an elongated shape and is composed of a central, alpha-helical domain that includes a distal alpha/beta domain and a proximal six-stranded SH3-like domain. The protomers assemble into a 12-mer, funnel-like structure with a 40 A wide central channel. The surface of the channel is mainly electronegative, but it includes three positively charged rings, one at the opening of the funnel, second at the middle of a particle and the third at the exit of the portal. We are looking to combine the crystal structure with macromolecular imaging in order to extensively characterize this portal structure.