HK97 PHAGE PORTAL

HK97 噬菌体门户网站

• 批准号: 8361120
• 负责人: ANDRZEJ JOACHIMIAK
• 金额: $ 1.23万
• 依托单位: BAYLOR COLLEGE OF MEDICINE
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-01-01 至 2011-12-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8361120
• 关键词: ATP Hydrolysis; Bacteriophage phi 29; Bacteriophages; Charge; DNA; DNA Packaging; Distal; Double Stranded DNA Virus; Electron Microscopy; Funding; Grant; Head; Image; Motor; National Center for Research Resources; Principal Investigator; Proteins; Protomer; Research; Research Infrastructure; Resolution; Resources; Shapes; Source; Structure; Surface; System; Tail; United States National Institutes of Health; Virus Assembly; cost; ds-DNA; macromolecule; monomer; particle; viral DNA

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.

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 而子项目的主要调查员可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 在大dsDNA病毒组装期间，病毒DNA被转移到预先形成的蛋白质壳中。 DNA包装由ATP驱动的易位马达系统驱动进入外壳 水解包装机的一个关键部分是门户蛋白。迄今为止， 详细的门户结构信息，因为只有两个门户噬菌体SPP 1和phi*29 门户已经确定。我们已经确定了双- 链DNA噬菌体HK 97样连接子至2.9 A分辨率。 这种400 kDa的马达蛋白将噬菌体的头部连接到其尾部，并将噬菌体的尾部转位。 DNA在包装过程中进入探头。 每个单体具有细长形状， 由包括远端α/β结构域和远端α/β结构域的中心α-螺旋结构域组成， 近端六链SH 3样结构域。原聚体组装成一个12聚体的漏斗状 一个40 A宽的中央通道。渠道的表面主要是 它是电负性的，但它包括三个带正电的环，一个在环的开口处， 漏斗，第二个在粒子的中间，第三个在入口的出口。 我们希望将晶体结构与大分子成像联合收割机相结合， 广泛地描述了这个门户结构。