CRYSTAL STRUCTURE OF COLB

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。所有的粘菌素都可以排列成三个功能结构域。氨基末端区域是跨外膜转运所必需的。中央结构域是识别外膜受体所必需的，而羧基末端结构域包含粘附素的杀伤活性。这些杀伤功能从核酸内切酶到抑制肽聚糖的合成，再到通过形成通道来使细胞膜失能。Colicin B通过Fepa进入细胞，通过在细胞质膜上形成通道来杀死细胞。我的实验室对通道形成粘菌素的杀灭作用很感兴趣。关于不同粘附素的通道形成结构域在体外在脂双层中的作用方式，已经有了很多确定。对于B类粘菌素，在体内所做的工作很少，而且没有任何晶体结构的好处来指导理解和突变。因此，Colicin B是结晶和我们进一步研究的极佳候选者。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. All colicins can be arranged into three functional domains. The amino terminal region is required for translocation across the outer membrane. The central domain is required for recognition of the outer membrane receptors and the carboxy terminal domain contains the killing activity of the colicin. These killing functions range from endonucleases to inhibition of peptidoglycan synthesis, to deenergizing cytoplasmic membranes by channel formation. Colicin B enters the cell through FepA, kills cells by forming channels in the cytoplasmic membrane. My lab is interested in the killing action of the channel-forming colicins. Much has been determined about the means by which the channel-forming domains of various colicins behave in vitro in lipid bilayers. With B-group colicins, very little work has been done in vivo, and that without benefit of any crystal structures to guide understanding and mutagenesis. Colicin B is thus an excellent candidate for crystallization and our further studies.