STRUCTURE AND MECHANISM OF YAET

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 这个项目的重点是确定YaeT蛋白的结构，这是YaeT复合体的中心成分，负责将蛋白质插入细菌外膜。干扰这种外膜蛋白插入机制将是抗生素开发的有效策略；就像β-内酰胺类药物一样，它通过抑制细胞壁合成而有效。YaeT由一个嵌入外膜的C-末端的β-桶和一个N-末端的周质结构域组成，该结构域包含五个所谓的POTRA(多肽运输相关)序列基序。我们测定了一个含有4个POTRA结构域的周质YaeT片段的晶体结构。

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. This project is focused on determining the structure of the YaeT protein, which is the central component of the YaeT complex responsible for insertion of proteins in the bacterial outer membrane. Interfering with this mechanism of Outer Membrane Protein insertion would be an effective strategy for antibiotic development; much like beta-lactams are effective by inhibiting cell wall synthesis. YaeT consists of a C-terminal beta-barrel embedded in the outer membrane, and an N-terminal periplasmic domain containing five copies of so-called POTRA (polypeptide-transport-associated) sequence motifs. We have determined the crystal structure of a periplasmic YaeT fragment containing 4 POTRA domains.